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Chitin Research Revisited

Feisal Khoushab, Montarop Yamabhai

Marine Drugs · 2010 · Review · CC BY

doi:10.3390/md8071988

Abstract

Two centuries after the discovery of chitin, it is widely accepted that this biopolymer is an important biomaterial in many aspects. Numerous studies on chitin have focused on its biomedical applications. In this review, various aspects of chitin research including sources, structure, biosynthesis, chitinolytic enzyme, chitin binding protein, genetic engineering approach to produce chitin, chitin and evolution, and a wide range of applications in bio- and nanotechnology will be dealt with.

Full text

From PubMed Central, U.S. National Library of Medicine, as current on Oct 20, 2026. Paragraph numbers are ours, so an answer can point at one.

1. Introduction

Chitin is one of the most abundant renewable biopolymer on earth that can be obtained as a cheap renewable biopolymer from marine sources. It is biocompatible, biodegradable and bio-absorbable, with antibacterial and wound-healing abilities and low immunogenicity; therefore there have been many reports on its biomedical applications. Accordingly, a very broad range of applications in different fields such as food technology, material science, microbiology, agriculture, wastewater treatment, drug delivery systems, tissue engineering, bionanotechnology have been reported.

Henri Braconnot, a French professor of natural history, discovered chitin in 1811 after the discovery of a “material particularly resistant to usual chemicals” by A. Hachett, an English scientist in 1799, and in 1843 Lassaigne demonstrated the presence of nitrogen in chitin. Henri Braconnot’s name for chitin was fungine. In 1823, Odier found the same material in insects and plants and named it chitine. Since all chitin-based materials are derivatives of chitin, in this paper the word chitin is used generally to describe both chitin and its derivatives unless otherwise mentioned in the text.

2. Source

Chitin, a poly-beta-1,4-N-acetylglucosamine (GlcNAc), is the main component of arthropod exoskeletons, tendons, and the linings of their respiratory, excretory, and digestive systems. It is also found in the reflective material (iridophores) both in the epidermis and the eyes of arthropods and cephalopods (phylum: Mollusca). Chitin is also an important component of the cell wall of fungi. Moreover, there is one report - based on lectin binding, endo-chitinase binding and enzymatic degradation studies - that the epidermal cuticle of a vertebrate named Paralipophrys trigloides (fish) is chitinous. Therefore, chitin is not only an essential component of invertebrates but may also be present in vertebrates. Unlike cellulose, chitin can be a source of nitrogen as well as carbon (C:N = 8:1).

3. Structure

Chitin contains 6–7% nitrogen and in its deacetylated form, chitosan contains 7–9.5% nitrogen. In chitosan, between 60 to 80% of the acetyl groups available in chitin are removed. There are three forms of chitin: α, β, and γ chitin. The α-form, which is mainly obtained from crab and shrimp shells, is widely distributed. Both α and β chitin/chitosan are commercially available. The α-chitin chains are aligned in anti-parallel fashion. The anti-parallel arrangement in α-chitin gives rise to strong hydrogen bonding and consequently makes it more stable. The β-form mainly obtained from mollusks such as squid, is arranged in parallel, whereas the γ-form contains two parallel and one anti-parallel strands of chitin. Conversion from the β-form to the α-form is possible, but not the reverse. γ chitin can be converted to α chitin by treatment with lithium thiocyanate.

Chitin is insoluble in water due to its intermolecular hydrogen bonds. But water-soluble chitin-based derivatives such as chitosan or carboxymethyl chitin can be obtained. One of their most important features is the ability (flexibility) to be shaped into different forms such as fibers, hydrogels, beads, sponges, and membranes. The origin of chitin affects its crystallinity, purity, polymer chain arrangement, and dictates its properties.

4. Chitin Biosynthesis

Chitin biosynthesis has been studied in a large variety of organisms. The enzyme for this synthesis is called chitin synthase (CS). Three CSs have been found in Saccharomyces cerevisiae CS I, CS II, and CS III. They are different from each other in terms of function and catalytic activity. Most of chitin is synthesized by CS III. Fungal CS are grouped into two families and five classes. There are two CS genes in insects. Nematodes possess two chitin synthase genes, which are differentially expressed. Therefore, there seems to be specialization among chitin synthases in different organisms where different enzymes carry out different functions. CSs use UDP-N-acetylglucosamine as substrate to produce chitin fibrils. This was proven in an experiment done on Mucor rouxii. The genomes of some chloroviruses contain a chitin synthase gene (cs). By introducing the gene of chlorovirus CVK2 into Chlorella cells, an algae that does not possess a chitin synthase gene, this microorganism could be engineered to produce chitin.

Several enzymes, so called DG, have been isolated from the Xenopus laevis embryos that are differentially expressed during the gastrulation stage. One of these enzymes is DG42. It is expressed from midblastula to the end of the neuralation stages. DG42 synthesizes a Nod-like chitin oligosaccharide. Nod is the enzyme responsible for producing chito-oligosaccharide in Rhizobium. It seems that while this enzyme is expressed during early embryogenesis the amount of hyaluronic acid (HA) increases. It has been suggested that chitin oligosaccharides are present at the reducing ends of HA chains. Thus, it has been proposed that chitin oligosaccharide produced by this enzyme acts as a primer for synthesizing HA. Homologs of DG42 have been found in zebrafish and mice. They also synthesize Nod-like chitin oligosaccharide during early embryogenesis. However, it remains controversial whether DGs are chitin synthase or hyaluronan synthase. Since DG42 has been isolated from frogs, zebrafish and most importantly mice, further study is needed to investigate whether or not this enzyme is widespread throughout mammals including humans, and if DGs is shown to synthesize chitin in animal, the role of chito-oligosaccharide in embryonic development should be further investigated.

5. Chitinolytic Enzymes

Chitinases, which hydrolyze chitin, are present in a wide range of organisms including viruses, bacteria, fungi, insects, higher plants, and mammals. Most organisms (bacteria, plants and insects) have large families of chitinases with distinct functions, including digestion, cuticle turnover, and cell differentiation. Based on amino acid sequence similarity they can be grouped into glycosyl hydrolase families (GH) 18 and 19, which are structurally unrelated. The catalytic mechanism of chitinases family 18 involves substrate-assisted catalysis, which retains the anomeric configuration of the product. They are ubiquitous with an (alpha/beta) 8-barrel fold structure in the catalytic domain. Family 19, glycosyl hydrolases, share a homologous catalytic domain. They consist mainly of alpha helices. Their catalytic mechanism is a general acid-base mechanism that inverts the anomeric configuration of the hydrolyzed GlcNAc residue. Family 19 chitinases have mostly been identified in plants. Both GH 18 and 19 chitinases have signal peptides, indicating that the enzymes are secreted and function outside the cells.

Family 18 of glycosyl hydrolases include active chitinases and inactive chitinase-like proteins or chito-lectins, which lack endogenous chitin and have been found widely in mammals. Recent comparative genomic analysis to address the evolutionary history of the GH18 multiprotein family from early eukaryotes to mammals, revealed that the GH18 chitinase involved in an emerging interface of innate and adaptive immunity during early vertebrate history. Chito-lectins are inactive due to lack of some critical residues in their catalytic sites. Several of these chitinase-like proteins have been identified such as oviductin or oviduct-specific glycoprotein, YKL-39, HC gp39 and YKL-40 in human, YM1, YM2, ECFL, breast regression protein 39 (BRP39) in mice, and gp38K in pigs. Their functions are unknown, however, it is speculated that they may be involved in fertilization, chemotaxis, and tissue remodeling. Besides these inactive chitinases, two active chitinases have been found in humans, these are chitotriosidase and acidic mammalian chitinase (AMCase). Chitotriosidase can cut both chitin oligomer and colloidal chitin; its optimum pH is broad, and it is mainly secreted from macrophages. AMCase is active in acidic pH, it is mostly expressed in stomach and lung, its gene has 11 exons and is located on chromosome 1. Interestingly, Glyco_18-containing proteins are established biomarkers for human diseases, and both human chitinases and chitinase-like proteins have been used as indicators of inflammation and cancer.

Bacterial chitinases belong to both family GH18 and 19. Most of their structure-function studies came from the studies of the enzymes from Serratia marcescens, B. circulans, and Vibrio spp..

Recently, chitinases have gained interest in different biotechnological applications due to their ability to degrade chitin in the fungal cell wall and insect exoskeleton, leading to their use as antimicrobial or insecticidal agents.. Another interesting application of chitinase is for bioconversion of chitin, a cheap biomaterial, into pharmacological active products, namely N-acetylglucosamine and chito-oligosaccharides. Production of chitin derivatives with suitable enzymes is more appropriate for sustaining the environment than using chemical reactions. Other interesting applications include the preparation of protoplasts from filamentous fungi, bio-control of insects and mosquitoes as well as the production of single cell protein. Thus, there have been many reports on cloning, expression and characterization of chitinases from various organisms, including bacteria, fungi, plant and animals.

6. Chitin Binding Proteins

Kawabata et al. identified a molecule, named tachycitin, from hemocytes of a horseshoe crab with chitin binding activity. This is a small molecule that is 73 residues long and possesses five disulfide bonds. A major protein in the chitin-walled cyst of protozoan Entamoeba histolytica also contains chitin binding domains. This protein is a lectin named EiJacob1. In addition, a chitin binding lectin has been isolated from Stinging Nettle Rhizomes. Several genes encoding proteins with chitin binding domains from arthropods have been identified by whole genome sequence analysis. Two proteins with chitin-binding domains have been identified from silkworm, Bombyx mori. In addition, it has been shown that Tribolium castaneum, red flour beetle, contains genes encoding proteins peritrophin A-type chitin-binding domains.

Chitin binding proteins have also been isolated from plants. They belong to the lectin superfamily and are secreted from the plants as a part of their defense system. Most of plant chitin binding proteins have a conserved motif, called havein domain or chitin binding domain.

A chitin binding protein with antifungal activity has been isolated and characterized from Streptomyces tendae Tü901. This protein binds to the surface of germinated conidia and tips of growing hyphae, changing the growth polarity of the fungi. Other organisms in which chitin binding proteins have been identified include sweet potato hornworm, Agrius convolvuli, Amaranthus caudatus, Ginkgo biloba, and Streptomyces reticuli. There is a conserved motif, known as RR consensus motif in the arthropods cuticular proteins, which along with its extended forms, are considered as chitin binding motifs.

Various chitinolytic microorganisms have been shown to produce non-hydrolytic accessory proteins that increase enzyme efficiency, such as the Gram-negative soil bacterium Serratia marcescens, which uses three different family 18 chitinases to degrade chitin. It has been reported that a small non-catalytic protein, CBP21, which binds to the insoluble crystalline substrate, leading to structural changes in the substrate and increased substrate accessibility, is required for efficient chitin degradation.

7. Genetic Engineering Approach to Produce Chitin

It is difficult to obtain pure carbohydrates, especially chitin, through conventional techniques. Bacterial cells have been engineered in an effort to overcome this problem. E. coli has been engineered to produce chitobiose. This method took advantage of NodC, which is a chito-oligosaccharide synthase, and genetically engineered chitinase to make a cell factory with the ability to produce chito-oligosaccharides. Recombinant chito-oligosaccharides have also been obtained using E. coli cells which expressed nodC or nodBC genes. By expressing different combinations of nod genes in E. coli, O-acetylated and sulfated chito-oligosaccharide have been produced.

8. Chitin and Evolution

There are several reports indicating that chitin plays a role not only in those organisms in which its role is expected, such as in fungi and crustaceans, but also in other organisms. It has been shown that Rhizobia-mediating nitrogen-fixing nodules possess a signal molecule necessary for the root nodulation process termed lipo-chitin oligosaccharide, which comprises a β-1,4-linked N-acetylglucosamine (GlcNAc) tetra- or penta-saccharide. N-acetylglucosamine has been reported to play a role during development of moulds as well.

The presence of intracellular and extracellular GlcNAc-containing compounds, in the forms of N-glycans and intracellular glycans, indicates the role of chitin and its derivatives from an evolutionary point of view. Finding a role for chitin derivatives in animals was an important discovery. Semino et al. (1997) proved the importance of chitin oligosaccharides in the embryogenesis of zebrafish and carp. GlcNAc containing muscle cell surface molecules have been shown to possess the ability to guide neurites through extracellular matrix. It has been reported that the addition of O-linked GlcNAc (O-GlcNAc) to the proteins in nucleus and cytoplasm is different from classical O-glycosylation of the secretory pathways. This reversible post-translational modification modifies serine and threonine residues and seems to play an important role in apoptosis, death signaling of mouse embryonic neuroepithelial cell, neurodegenerative disorders, signal transduction, synaptic plasticity, transcription and translation, stability of target proteins, proteasomal function, cancer, diabetes, subcellular localization, and nuclear transport. O-GlcNAc is also important in the cardiovascular, and immune systems. Considering the fact mentioned in part 4 about the role of chitin synthase and chitin-oligomer in mice, which is close to human species, and that humans have chitinase genes, it would not be surprising if future studies found one or more roles for chitinous materials in humans at some point in human evolution and/or embryonic development.

9.1. Immunology

The key property of chitin-derived products for application in various biomedical applications is the immuno-modulating effect. Various mechanisms of immuno-enhancement activity of chitin and its derivatives have been reported. For example, chitosan exhibited the ability to boost NO production from macrophages in the presence of interferon-γ (IFN-γ) through the NF-κB signaling pathway. In addition, Minami et al. (1998) found that chitin and chitosan affected C3 and C5 components of complement system and concluded that complement system is activated by chitin and chitosan through the alternative pathway. After activating the complement, C5a is produced followed by an increase in migration of polymorphonucleate (PMN) to the injured tissue. This is a normal inflammatory reaction but in the presence of chitin and chitosan, there are no inflammatory symptoms, such as erythema, temperature elevation and abscess formation. The intensity of complement and macrophage activation of chitin is less than chitosan; therefore, chitin is more biocompatible.

9.2. Hemostasis and Wound Healing

Hemostasis through blood coagulation is an important step for wound healing. The main cellular components in blood coagulation are platelets. It has been shown that chitosan has a hemostatic effect. Okamoto Y. et al. reported that chitin is an effective agent for hemostasis maintenance through aggregating platelets, and suggested that the effect of chitin and chitosan is due to both physical and chemical properties of these biopolymers, especially their amino groups. Shelma et al. (2008) developed a composite film by using chitosan and chitin. They used chitin nano-fiber to improve the composite’s tensile strength and elasticity. Mi et al. designed an asymmetric chitosan membrane with the ability to protect skin by preventing bacterial invasion and halting the evaporation of the skin’s water, two important factors for dressing wounded skin. A chitosan acetate bandage has been shown to have good antibacterial activity when applied to burnt skin contaminated with P. aeruginosa.

9.3. Scaffold for the Regeneration of Tissue

Chitin and its derivatives have been used as scaffolds for bone and other natural tissue regeneration as well as structures by which three-dimensional formation of tissues are supported. While looking for a good material for a good scaffold, there are at least four important factors that should be taken into account: (1) ability to form temporary matrix, (2) ability to form porous structure for tissue to grow, (3) biodegradability, and finally (4) non-toxic byproducts from the digestion. Thus, neither the physical nor biological properties of such biomaterials should be ignored. Chitin and its derivatives have been shown to possess these criteria.

9.4. Neuro-Tubes Guided Nerve Regeneration

Based on the fact that chitin has high mechanical strength under physiological conditions (low for chitosan) chitin has the potential to be a good nerve guidance channel. Ferier et al. used this fact and made chitin tubes that could support nerve cell adhesion and neurite outgrowth. In a research related to nerve regeneration, it was shown that rabbits with the crushed common peroneal nerve exhibit better improvement in peripheral nerve regeneration in the presence of chitooligosaccharide. As a result, chito-oligosaccharide can be used as neuroprotective material with an ability to improve injured peripheral nerve regeneration.

9.5. Blood Cholesterol Control

Chitin and chitosan are among the candidates to battle obesity and hypercholesterolemia. It has been reported that they can reduce the amount of cholesterol in rats. Several mechanisms have been proposed to explain this phenomenon. One is through electrostatic interaction between lipids and aminopolysaccharides. Chitin binds to lipid (cholesterol) micelles and inhibits their absorption. Another proposed mechanism is increasing the excretion of bile acid by which the amount of fecal fat increases. Feeding mice with chitosan showed hypocholesterolemic effects. It seems that the mechanism of chitosan’s cholesterol-lowering effect is through suppression of food intake. The hypocholesterolemic effect of chitosan has also been found in humans. When 3–6 g/day of chitosan was given in the diet to eight healthy males, total serum cholesterol significantly decreased, and when the ingestion was stopped, the value increased to the level before ingestion. The proposed cholesterol lowering mechanism of chitosan was that it combines bile acids in the digestive tract, and excretes them into the feces, thus decreasing the resorption of bile acids, so that the cholesterol pool in the body was decreased and the level of serum cholesterol consequently decreased.

9.6. Drug Delivery Carriers

It is important for a drug delivery carrier to be efficiently removed after delivering drugs. In other words, it must not accumulate in the body nor must it be toxic. Chitin derivatives such as N-succinyl-chitosan, carboxymethyl chitin, chitosan hydrogel, and hydroxyethyl chitin have been shown to possess such characteristics.

Chitosan in the form of colloidal structures can entrap macromolecules by various mechanisms. These associated macromolecules have been shown to transport through mucosa and epithelia more efficiently. Cationic chitosan in combination with other natural polymers has been shown to enhance the drug encapsulation efficiency of liposomes via the layer-by-layer (L-b-L) self-assembly technique. Nanoparticles made of chitosan in association with polyethylene oxide have been used as protein carrier. Moreover, an oral delivery system has been developed by using chitosan and tripolyphosphate. In this system, micro- and nano-particles were entrapped in beads made from chitosan in solution of tripolyphosphate.

9.7. Antioxidant

The balance between oxidant formation and antioxidant defense in biological systems is important in order to prevent oxidation of biomolecules. The higher oxidation activity in cells, which leads to a higher potential for cell injury, is the cause of cancer, arthritis, neurodegeneration, and aging. Chitin and its derivatives have been reported to have antioxidant properties, hence preventive effects on various diseases.

Chitin that was chemically modified to obtain aminoethyl-chitin, showed antioxidant activity against free radicals such as 1,1-diphenyl-2-picrylhydrazyl (DPPH), hydroxyl, superoxide, and peroxyl. In addition, the antioxidant activity of hetero-chitosan has been shown to depend on its deacetylation degree and concentration. It seems that free amino groups play a major role in antioxidant activity of chitinous materials. The proposed mechanism behind this activity is that the free radicals react with NH2 groups and these groups absorb hydrogen ion from the solution to produce NH3 groups.

9.8. Antimicrobial Activity

Antifungal and antibacterial activities of chitinous products have been demonstrated in several articles. For example, S. Bautista-Baños et al. reported the antifungal activity of chitosan against Colletotrichum gloeosporioides, which causes anthracnose in papaya. Chitosan has been reported to possess the antibacterial ability against E. coli through cross-linking between chitosan (as cation) and anions over the surface of E. coli. It has been shown that culture broth of Bacillus subtilis grown in the presence of chitin exhibits antifungal activity on pathogenic Fusarium oxysporum, indicating that it can be used as a bio-control agent. In addition, chitosan solution has been shown to inhibit the growth of Xanthomonas sp., which is pathogenic to Euphorbia pulcherrima.

The mechanism of antifungal and antimicrobial activity of chitin and its derivatives has yet to be totally uncovered. In fact there are several proposed mechanisms. One of them is the ability of chitin and its derivatives to activate defense mechanisms of the host organisms such as inducing the accumulation of chitinases and other pathogenesis-related proteins. Another one is leakage in the cell wall of bacteria due to the interaction between positively charged chitosan molecules and the negatively charged surface of the bacteria.

9.9. Gene Therapy

Being able to deliver a large piece of DNA plays an important role in gene therapy. The carrier must be safe with low immunogenicity. One of the carriers being used—viral vectors—may not be safe enough for targeting cells. Cationic derivatives of chitin are being used to serve this purpose. Galactosylated chitosan has been grafted to dextran to make a liver-specific DNA carrier. Another group has synthesized nanosphere delivery vehicle by salt-induced complex co-acervation of cDNA and chitosan. Chitosan can condense DNA and forms small discrete particles in particular conditions; hence it has many potential applications for gene delivery.

9.10. Food Technology

Chemical preservatives can be replaced with chitin-based ones. The advantages are two-fold. First, chitinous materials are safer, and second, with their antimicrobial activity; they can protect food products against microbial invasion. Chitosan-based films have been developed to serve this purpose. It has also been applied to improve the preservation of vacuum-packaged processed meat and it could delay the growth of Entrobacteriaceae, which are indigenous bacteria in the food products. It seems this antibacterial activity is due to the positive charge of C2 amino group in glucosamine, monomer of chitosan. This positive charge interacts with negatively charged microbial cell membrane and leads to leakage of the intracellular constituents of the microorganisms.

9.11. Agriculture

Chitin oligosaccharides have been shown to play an important role in defense mechanisms of plants against microbial invasion. They could also promote carrot somatic embryos survival. Chitin fragments can desensitize the perception system of tomato, which can lead to improvement of the defense mechanism in tomato cells. Chitin in the form of lipo-chitin can induce the formation of nodule in soybean root. Rice is another important plant in which chitin fragments have been shown to boost the defense system.

9.12. Bio-Nanotechnology

Bio-nanotechnology, a marriage between biology and nanotechnology, is an emerging field. Through biomimetic approaches and strategies, many micro/nano-systems can be produced. Chitosan has been used to immobilize and pattern biomolecules on microfabricated surfaces. A photolithographic method has been applied to integrate chitosan to micro- and nano-structures, which is an important step toward the fabrication of bioinspired micro-electromechanical systems. Nanoimprinting lithography was used to micro- and nano-pattern chitosan. This micro/nanopatterning enables researchers to use chitosan for bionanotechnology applications such as nanobiodevices. Chitiosan has recently been used in the preparation of graphitic carbon nanocapsules, tungsten carbide and tungsten carbides/graphitic carbon composites. In this system, after preparation of the precursors of chitosan and metal ions, they were carbonized. The system can be regulated by changing the type and/or ratio of the metal. Chitin whiskers have been used to reinforce nanocomposites. It seems this ability mainly depends on chitin whiskers being able to form 3D networks. Any modification by which this network is disrupted results in lowering or loss of this ability.

9.13. Capacitor and Electrolyte

Electric double layer capacitors are being used as memory back-up tools and energy storage technology. Electrolytes used in these capacitors should have low internal resistance and high capacitance. There are two type of electrolytes; aqueous and nonaqueous. Aqueous electrolytes have high electrical conductivity. KOH and H2SO4, which are being used to make aqueous electrolytes, are strong base and acid, and thus are hazardous and difficult to handle. It is important to have less toxic or non-toxic aqueous electrolytes that are stable and exhibit good conductivity and low resistance. Yamazaki et al. made a gel using a mixture of cellulose, chitin, and H2SO4, which has all the mentioned features as well as high charge-discharge ability.

9.14. Heavy Metals and Other Pollutants Removal

The wide usage of heavy metals in industry has caused and continues to cause serious and widespread health problems. It is important to remove these metals from the environment. Several studies have reported the ability of chitin and chitosan to perform this task. For instance, absorbing Cu (II) and Cr (VI), Fe, and Pb (II) ions in an aqueous environment. Chitin phosphate could absorb uranium in the presence of sodium carbonate solution. Chitosan-based chelating resins have been developed to absorb mercury, Ti (IV), V (V), Mo (VI), W (VI), U (VI), Ag in aquatic environment, Cd, Ni, V, Ga, Sc, In, and Th. Chitin and chitosan have been shown to have copper removal capability, which could help to obtain more stable diesel oil. They also have been successfully tested for the adsorption of organic pollutants.

9.15. Intelligent Materials or Composites

Chitinous materials have been used to create smart or intelligent materials or composites. These systems can respond to environmental changes. They show their functionality with the addition or removal of stimulation. These smart or intelligent materials are ideal in an integrated systems or mixed composite of materials. Shape memory materials are one group of such materials. As is obvious from the name, shape memory materials can remember and regain their original shape after the removal of the stimulus. This phenomenon is due to their being equipped with proper stimulus sensitive molecular switches. Among these shape memory materials, polyurethanes are gaining more attention. This is because of their good shape memory effect at room temperature as well as their low cost. But shape memory polyurethanes cannot bear repeated changes in the shape memory, and retention will decrease by increasing the number of cycles of shape memory; consequently, chitin-based polyurethane shape memory materials have been developed to overcome these problems.

9.16. Energy Production: An Emerging Application

Insects are widely distributed on earth, comprising 80% of species. Robots with the ability to hunt and digest insects and obtain energy from them can serve humanity by performing missions in dangerous situations. A robot that contains a microbial fuel cell was created to digest chitin and metabolize it by bacteria. This process produces electrons that act as horsepower of the system. The system can take advantage of the wide distribution of arthropods and mollusks because chitin is available in both phyla. Since Arthropoda and Mollusca rank first and second in species diversity in all animal phyla and are a major source of chitin, this strategy can be highly applicable in both land and marine environments. Chitin has also been utilized by Clostridium paraputrificum M-21 to produce hydrogen gas. This gas is considered to be a potential source of alternative energy. The advantage of using chitin in this way is that most chitin sources are waste materials, such as shrimp shells; therefore, it is non-food material and there is no need to be concerned about pressure on food supplies.

10. Chito-Oligosaccharides and Their Applications

Recent trends in the field of chitin research have focused on oligosaccharides, which are more soluble and have several attractive biological effects. N-acetylchitooligosaccharide and chitooligosaccharide (COS) are originated from chitin and chitosan, respectively. Oligomers of chitin and chtitosan can be obtained both chemically and enzymatically. Their degree of polymerization (DP) is usually < 20.

It has been shown that chito-oligosaccharide accelerates the wound healing effects of Poly vinyl alcohol (PVA) if it is used in the early stages of the healing process. It could inhibit the growth of Actinobacillus actinomycetemcomitans, indicating that it has antimicrobial activity. N-acetylchitooligosaccharide causes an increase in biophotons emission from suspension-cultured rice cells. Biophotons are very weak light emitted from biological processes/systems. All organisms, including plants, constantly produce biophotons as part of their vital activities. Photon emissions are elevated by environmental stresses and disease responses induced by pathogen attack. It has been shown that photon emissions from rice cells elicited by N-acetylchitohexaose are closely associated with the ROS-generating system, and are regulated by Ca2+ signaling and protein phosphorylation via phosphatidic acid (PA), an intermediate of phospholipid signaling. Chito-oligosaccharide has shown inhibitory effects on tumor growth and metastasis of lung cancer in mice. N-acetylchitohexaose (chitin derivertive) and chitohexaose (chitosan derivertive) can also induce production of interleukins 1 and 2 and, consequently, help to improve the function of macrophages, natural killers, cytotoxic T cells, and polymorphonuclear leukocytes, in defense mechanisms. The anti-metastatic activity of acetylchitohexaose against Lewis lung carcinoma in mice has been demonstrated. There are many reports indicating antitumor activity of chito-oligosaccharides. It has been shown that oligosaccharides that contain N-acetylglucosamine play an important role in the interaction between HIV and T-helper during pathogenesis of this virus. N-acetylchitooligosaccharide was used as analogue to study lysozyme. Thus, these materials can be used to study protein-carbohydrate interaction and associated enzymatic activities.

11. Conclusion and Future Perspectives

After two centuries of research on chitin, this biopolymer now has applications in numerous fields, as described in many review articles. However, there is still room for further chitin research. Chitin is a potential energy source as well as gene and drug delivery carrier, and in the emerging field of nanobiotechnology. The evolutionary effects of chitin is emerging, but is not yet fully discovered. To take advantage of the mechanical characteristics of chitin, it should be used directly and without chemical modification. To achieve this goal, more research, especially on fundamental aspects, needs to be done.

Much attention has being paid to chitinase research, but its substrate seems to have been neglected or, at least, underestimated. If we are going to use the huge amount of chitin produced annually in nature, chitin research needs an increase in funding to develop equipment to harvest chitin from its diverse sources, improve the purity of obtained chitin, and produce novel materials with new applications from this environmentally friendly biopolymer.

Despite the multiple potential applications of chitin, we believe that the most promising in the future are (i) applications in nanobiotechnology, which involves drug and gene delivery and scaffold for tissue engineering, and (ii) applications of chito-oligosaccharides in medicine and agriculture.

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  18. 18.

    Mano JF Silva GA Azevedo HS Malafaya PB Sousa RA Silva SS Boesel LF Oliveira JM Santos TC Marques AP Neves NM Reis RL Natural origin biodegradable systems in tissue engineering and regenerative medicine: present status and some moving trendsJ. R. Soc. Interface2007 49991030

    Not in our library10.1098/rsif.2007.0220

  19. 19.

    Rinaudo M Chitin and chitosan: Properties and applicationsProg. Polym. Sci2006 31603632

    Not in our library

  20. 20.

    Bulawa CE Genetics and Molecular Biology of Chitin Synthesis in FungiAnnu. Rev. Microb1993 47505534

    Not in our library10.1146/annurev.mi.47.100193.002445

  21. 21.

    Roncero C The genetic complexity of chitin synthesis in fungiCurr. Genet2002 41367378

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  22. 22.

    Merzendorfer H Insect chitin synthases: a reviewJ. Comp. Physiol. B2006 176115

    Not in our library10.1007/s00360-005-0005-3

  23. 23.

    Kato N Mueller CR Fuchs JF Wessely V Lan Q Christensen BM Regulatory mechanisms of chitin biosynthesis and roles of chitin in peritrophic matrix formation in the midgut of adult Aedes aegyptiInsect. Biochem. Mol. Biol2006 3619

    Not in our library10.1016/j.ibmb.2005.09.003

  24. 24.

    Veronico P Gray LJ Jones JT Bazzicalupo P Arbucci S Cortese MR Di Vito M De Giorgi C Nematode chitin synthases: gene structure, expression and function in Caenorhabditis elegans and the plant parasitic nematode Meloidogyne artielliaMol. Genet. Genomics2001 2662834

    Not in our library10.1007/s004380100513

  25. 25.

    Cohen E Chitin synthesis and inhibition: a revisitPest Manag. Sci2001 57946950

    Not in our library10.1002/ps.363

  26. 26.

    McMurrough I Flores-Carreon A Bartnicki-Garcia S Pathway of chitin synthesis and cellular localization of chitin synthetase in Mucor rouxiiJ. Biol. Chem1971 24639994007

    Not in our library

  27. 27.

    Kawasaki T Tanaka M Fujie M Usami S Sakai K Yamada T Chitin Synthesis in Chlorovirus CVK2-Infected Chlorella CellsVirology2002 302123131

    Not in our library10.1006/viro.2002.1572

  28. 28.

    Lerouge P Roche P Faucher C Maillet F Truchet G Prome JC Denarie J Symbiotic host-specificity of Rhizobium meliloti is determined by a sulphated and acylated glucosamine oligosaccharide signalNature1990 344781784

    Not in our library10.1038/344781a0

  29. 29.

    Semino CE Robbins PW Synthesis of "Nod"-like chitin oligosaccharides by the Xenopus developmental protein DG42Proc. Natl. Acad. Sci. USA1995 9234983501

    Not in our library10.1073/pnas.92.8.3498

  30. 30.

    Semino CE Specht CA Raimondi A Robbins PW Homologs of the Xenopus developmental gene DG42 are present in zebrafish and mouse and are involved in the synthesis of Nod-like chitin oligosaccharides during early embryogenesisProc. Natl. Acad. Sci. USA1996 9345484553

    Not in our library10.1073/pnas.93.10.4548

  31. 31.

    Hawtin RE Arnold K Ayres MD Zanotto PM Howard SC Gooday GW Chappell LH Kitts PA King LA Possee RD Identification and preliminary characterization of a chitinase gene in the Autographa californica nuclear polyhedrosis virus genomeVirology1995 212673685

    Not in our library10.1006/viro.1995.1525

  32. 32.

    Chigaleichik AG Pirieva DA Rydkin SS Chitinase from Serratia marcescens BKM B-851Prikl. Biokhim. Mikrobiol1976 12581586

    Not in our library

  33. 33.

    Kuranda MJ Robbins PW Chitinase is required for cell separation during growth of Saccharomyces cerevisiaeJ. Biol. Chem1991 2661975819767

    Not in our library

  34. 34.

    Sakuda S Isogai A Matsumoto S Suzuki A Search for microbial insect growth regulators. II. Allosamidin, a novel insect chitinase inhibitorJ. Antibiot. (Tokyo)1987 40296300

    Not in our library10.7164/antibiotics.40.296

  35. 35.

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    Not in our library

  36. 36.

    Nakazaki T Tsukiyama T Okumoto Y Kageyama D Naito K Inouye K Tanisaka T Distribution, structure, organ-specific expression, and phylogenic analysis of the pathogenesis-related protein-3 chitinase gene family in rice (Oryza sativa L.)Genome2006 49619630

    Not in our library10.1139/g06-020

  37. 37.

    Bussink AP Speijer D Aerts JM Boot RG Evolution of mammalian chitinase(-like) members of family 18 glycosyl hydrolasesGenetics2007 177959970

    Not in our library10.1534/genetics.107.075846

  38. 38.

    Cohen-Kupiec R Chet I The molecular biology of chitin digestionCurr. Opin. Biotechnol1998 9270277

    Not in our library10.1016/s0958-1669(98)80058-x

  39. 39.

    Coulson AF A proposed structure for 'family 18' chitinases. A possible function for narboninFEBS Lett1994 3544144

    Not in our library10.1016/0014-5793(94)01084-6

  40. 40.

    Itoh Y Kawase T Nikaidou N Fukada H Mitsutomi M Watanabe T Itoh Y Functional analysis of the chitin-binding domain of family 19 chitinase from streptomyces griseus HUT6037: substrate-binding affinity and cis-dominant increase of antifungal functionBiosci. Biotechnol. Biochem2002 6610841092

    Not in our library10.1271/bbb.66.1084

  41. 41.
    Chitinase family GH18: evolutionary insights from the genomic history of a diverse protein family · 2007
    No notice
  42. 42.

    Sendai Y Abe H Kikuchi M Satoh T Hoshi H Purification and molecular cloning of bovine oviduct-specific glycoproteinBiol. Reprod1994 50927934

    Not in our library10.1095/biolreprod50.4.927

  43. 43.

    Hu B Trinh K Figueira WF Price PA Isolation and sequence of a novel human chondrocyte protein related to mammalian members of the chitinase protein familyJ. Biol. Chem1996 2711941519420

    Not in our library10.1074/jbc.271.32.19415

  44. 44.

    Hakala BE White C Recklies AD Human cartilage gp-39, a major secretory product of articular chondrocytes and synovial cells, is a mammalian member of a chitinase protein familyJ. Biol. Chem1993 2682580325810

    Not in our library

  45. 45.

    Johansen JS Olee T Price PA Hashimoto S Ochs RL Lotz M Regulation of YKL-40 production by human articular chondrocytesArthritis Rheum2001 44826837

    Not in our library10.1002/1529-0131(200104)44:4<826::aid-anr139>3.0.co;2-u

  46. 46.

    Kirkpatrick RB Emery JG Connor JR Dodds R Lysko PG Rosenberg M Induction and Expression of Human Cartilage Glycoprotein 39 in Rheumatoid Inflammatory and Peripheral Blood Monocyte-Derived MacrophagesExp. Cell Res1997 2374654

    Not in our library10.1006/excr.1997.3764

  47. 47.

    Chang N-CA Hung S-I Hwa K-Y Kato I Chen J-E Liu C-H Chang AC A Macrophage Protein, Ym1, Transiently Expressed during Inflammation Is a Novel Mammalian LectinJ. Biol. Chem2001 2761749717506

    Not in our library10.1074/jbc.m010417200

  48. 48.

    Webb DC McKenzie ANJ Foster PS Expression of the Ym2 Lectin-binding Protein Is Dependent on Interleukin (IL)-4 and IL-13 Signal TransductionJ. Biol. Chem2001 2764196941976

    Not in our library10.1074/jbc.m106223200

  49. 49.

    Owhashi M Arita H Hayai N Identification of a Novel Eosinophil Chemotactic Cytokine (ECF-L) as a Chitinase Family ProteinJ. Biol. Chem2000 27512791286

    Not in our library10.1074/jbc.275.2.1279

  50. 50.

    Lee CG Hartl D Lee GR Koller B Matsuura H Da Silva CA Sohn MH Cohn L Homer RJ Kozhich AA Humbles A Kearley J Coyle A Chupp G Reed J Flavell RA Elias JA Role of breast regression protein 39 (BRP-39)/chitinase 3-like-1 in Th2 and IL-13-induced tissue responses and apoptosisJ. Exp. Med2009 20611491166

    Not in our library10.1084/jem.20081271

  51. 51.

    Shackelton LM Mann DM Millis AJT Identification of a 38-kDa Heparin-binding Glycoprotein (gp38k) in Differentiating Vascular Smooth Muscle Cells as a Member of a Group of Proteins Associated with Tissue RemodelingJ. Biol. Chem1995 2701307613083

    Not in our library10.1074/jbc.270.22.13076

  52. 52.

    Verhage HG Mavrogianis PA O'Day-Bowman MB Schmidt A Arias EB Donnelly KM Boomsma RA Thibodeaux JK Fazleabas AT Jaffe RC Characteristics of an oviductal glycoprotein and its potential role in the fertilization processBiol. Reprod1998 5810981101

    Not in our library10.1095/biolreprod58.5.1098

  53. 53.

    Johansen JS Studies on serum YKL-40 as a biomarker in diseases with inflammation, tissue remodelling, fibroses and cancerDan. Med. Bull2006 53172209

    Not in our library

  54. 54.

    Renkema GH Boot RG Muijsers AO Donker-Koopman WE Aerts JMFG Purification and Characterization of Human Chitotriosidase, a Novel Member of the Chitinase Family of ProteinsJ. Biol. Chem1995 27021982202

    Not in our library10.1074/jbc.270.5.2198

  55. 55.

    Boot RG Blommaart EFC Swart E Ghauharali-van der Vlugt K Bijl N Moe C Place A Aerts JMFG Identification of a Novel Acidic Mammalian Chitinase Distinct from ChitotriosidaseJ. Biol. Chem2001 27667706778

    Not in our library10.1074/jbc.m009886200

  56. 56.

    Boot RG Renkema GH Strijland A van Zonneveld AJ Aerts JM Cloning of a cDNA encoding chitotriosidase, a human chitinase produced by macrophagesJ. Biol. Chem1995 2702625226256

    Not in our library10.1074/jbc.270.44.26252

  57. 57.

    Krykbaev R Fitz LJ Reddy PS Winkler A Xuan D Yang X Fleming M Wolf SF Evolutionary and biochemical differences between human and monkey acidic mammalian chitinasesGene2010 4526371

    Not in our library10.1016/j.gene.2009.12.005

  58. 58.

    Kzhyshkowska J Gratchev A Goerdt S Human chitinases and chitinase-like proteins as indicators for inflammation and cancerBiomark Insights2007 2128146

    Not in our library

  59. 59.

    Kolstad G Synstad B Eijsink VG van Aalten DM Structure of the D140N mutant of chitinase B from Serratia marcescens at 1.45 A resolutionActa Crystallogr. D Biol. Crystallogr2002 58377379

    Not in our library10.1107/s0907444901018972

  60. 60.

    Vaaje-Kolstad G Houston DR Rao FV Peter MG Synstad B van Aalten DM Eijsink VG Structure of the D142N mutant of the family 18 chitinase ChiB from Serratia marcescens and its complex with allosamidinBiochim. Biophys. Acta2004 1696103111

    Not in our library10.1016/j.bbapap.2003.09.014

  61. 61.
    Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-Å resolution · 2000
    Not checked
  62. 62.

    Ferrandon S Sterzenbach T Mersha FB Xu MQ A single surface tryptophan in the chitin-binding domain from Bacillus circulans chitinase A1 plays a pivotal role in binding chitin and can be modified to create an elutable affinity tagBiochim. Biophys. Acta2003 16213140

    Not in our library10.1016/s0304-4165(03)00029-1

  63. 63.

    Hardt M Laine RA Mutation of active site residues in the chitin-binding domain ChBDChiA1 from chitinase A1 of Bacillus circulans alters substrate specificity: use of a green fluorescent protein binding assayArch Biochem. Biophys2004 426286297

    Not in our library10.1016/j.abb.2004.03.017

  64. 64.

    Jee JG Ikegami T Hashimoto M Kawabata T Ikeguchi M Watanabe T Shirakawa M Solution structure of the fibronectin type III domain from Bacillus circulans WL-12 chitinase A1J. Biol. Chem2002 27713881397

    Not in our library10.1074/jbc.m109726200

  65. 65.

    Watanabe T Uchida M Kobori K Tanaka H Site-directed mutagenesis of the Asp-197 and Asp-202 residues in chitinase A1 of Bacillus circulans WL-12Biosci. Biotechnol. Biochem1994 5822832285

    Not in our library10.1271/bbb.58.2283

  66. 66.

    Watanabe T Ariga Y Sato U Toratani T Hashimoto M Nikaidou N Kezuka Y Nonaka T Sugiyama J Aromatic residues within the substrate-binding cleft of Bacillus circulans chitinase A1 are essential for hydrolysis of crystalline chitinBiochem. J2003 376237244

    Not in our library10.1042/bj20030419

  67. 67.

    Watanabe T Kobori K Miyashita K Fujii T Sakai H Uchida M Tanaka H Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activityJ. Biol. Chem1993 2681856718572

    Not in our library

  68. 68.

    Songsiriritthigul C Pantoom S Aguda AH Robinson RC Suginta W Crystal structures of Vibrio harveyi chitinase A complexed with chitooligosaccharides: implications for the catalytic mechanismJ. Struct. Biol2008 162491499

    Not in our library10.1016/j.jsb.2008.03.008

  69. 69.

    Suginta W Songsiriritthigul C Kobdaj A Opassiri R Svasti J Mutations of Trp275 and Trp397 altered the binding selectivity of Vibrio carchariae chitinase ABiochim. Biophys. Acta2007 177011511160

    Not in our library10.1016/j.bbagen.2007.03.012

  70. 70.

    Suginta W Vongsuwan A Songsiriritthigul C Svasti J Prinz H Enzymatic properties of wild-type and active site mutants of chitinase A from Vibrio carchariae, as revealed by HPLC-MSFEBS J2005 27233763386

    Not in our library10.1111/j.1742-4658.2005.04753.x

  71. 71.

    Karasuda S Tanaka S Kajihara H Yamamoto Y Koga D Plant chitinase as a possible biocontrol agent for use instead of chemical fungicidesBiosci. Biotechnol. Biochem2003 67221224

    Not in our library10.1271/bbb.67.221

  72. 72.

    Mostafa SA Mahmoud MS Mohamed ZK Enan MR Cloning and molecular characterization of chitinase from Bacillus licheniformis MS-3J. Gen. Appl. Microbiol2009 55241246

    Not in our library10.2323/jgam.55.241

  73. 73.

    Tsujibo H Kubota T Yamamoto M Miyamoto K Inamori Y Characterization of chitinase genes from an alkaliphilic actinomycete, Nocardiopsis prasina OPC-131Appl. Environ. Microbiol2003 69894900

    Not in our library10.1128/aem.69.2.894-900.2003

  74. 74.

    Bhattacharya D Nagpure A Gupta RK Bacterial chitinases: properties and potentialCrit. Rev. Biotechnol2007 272128

    Not in our library10.1080/07388550601168223

  75. 75.

    Dahiya N Tewari R Hoondal GS Biotechnological aspects of chitinolytic enzymes: a reviewAppl. Microbiol. Biotechnol2006 71773782

    Not in our library10.1007/s00253-005-0183-7

  76. 76.

    Hayes M Carney B Slater J Bruck W Mining marine shellfish wastes for bioactive molecules: chitin and chitosan--Part B: applicationsBiotechnol. J2008 3878889

    Not in our library10.1002/biot.200800027

  77. 77.

    Songsiriritthigul C Pesatcha P Eijsink VG Yamabhai M Directed evolution of a Bacillus chitinaseBiotechnol. J2009 4501509

    Not in our library10.1002/biot.200800258

  78. 78.

    Howard MB Ekborg NA Weiner RM Hutcheson SW Detection and characterization of chitinases and other chitin-modifying enzymesJ. Ind. Microbiol. Biotechnol2003 30627635

    Not in our library10.1007/s10295-003-0096-3

  79. 79.

    Patil RS Ghormade VV Deshpande MV Chitinolytic enzymes: an explorationEnzyme Microb. Technol2000 26473483

    Not in our library10.1016/s0141-0229(00)00134-4

  80. 80.

    Songsiriritthigul C Lapboonrueng S Pechsrichuang P Pesatcha P Yamabhai M Expression and characterization of Bacillus licheniformis chitinase (ChiA), suitable for bioconversion of chitin wasteBioresour. Technol2010 10140964103

    Not in our library10.1016/j.biortech.2010.01.036

  81. 81.

    Kawabata S Nagayama R Hirata M Shigenaga T Agarwala KL Saito T Cho J Nakajima H Takagi T Iwanaga S Tachycitin, a small granular component in horseshoe crab hemocytes, is an antimicrobial protein with chitin-binding activityJ. Biochem1996 12012531260

    Not in our library10.1093/oxfordjournals.jbchem.a021549

  82. 82.

    Van Dellen KL Chatterjee A Ratner DM Magnelli PE Cipollo JF Steffen M Robbins PW Samuelson J Unique posttranslational modifications of chitin-binding lectins of Entamoeba invadens cyst wallsEukaryot. Cell2006 5836848

    Not in our library10.1128/ec.5.5.836-848.2006

  83. 83.

    Broekaert WF Van Parijs J Leyns F Joos H Peumans WJ A Chitin-Binding Lectin from Stinging Nettle Rhizomes with Antifungal PropertiesScience1989 24511001102

    Not in our library10.1126/science.245.4922.1100

  84. 84.

    Willis JH Structural cuticular proteins from arthropods: annotation, nomenclature, and sequence characteristics in the genomics eraInsect. Biochem. Mol. Biol2010 40189204

    Not in our library10.1016/j.ibmb.2010.02.001

  85. 85.

    Tang L Liang J Zhan Z Xiang Z He N Identification of the chitin-binding proteins from the larval proteins of silkworm, Bombyx moriInsect. Biochem. Mol. Biol2010 40228234

    Not in our library10.1016/j.ibmb.2010.01.010

  86. 86.

    Jasrapuria S Arakane Y Osman G Kramer KJ Beeman RW Muthukrishnan S Genes encoding proteins with peritrophin A-type chitin-binding domains in Tribolium castaneum are grouped into three distinct families based on phylogeny, expression and functionInsect. Biochem. Mol. Biol2010 40214227

    Not in our library10.1016/j.ibmb.2010.01.011

  87. 87.

    Selitrennikoff CP Antifungal ProteinsAppl. Environ. Microbiol2001 6728832894

    Not in our library10.1128/aem.67.7.2883-2894.2001

  88. 88.

    Asensio JL Canada FJ Siebert HC Laynez J Poveda A Nieto PM Soedjanaamadja UM Gabius HJ Jimenez-Barbero J Structural basis for chitin recognition by defense proteins: GlcNAc residues are bound in a multivalent fashion by extended binding sites in hevein domainsChem. Biol2000 7529543

    Not in our library10.1016/s1074-5521(00)00136-8

  89. 89.

    Bormann C Baier D Horr I Raps C Berger J Jung G Schwarz H Characterization of a novel, antifungal, chitin-binding protein from Streptomyces tendae Tu901 that interferes with growth polarityJ. Bacteriol1999 18174217429

    Not in our library10.1128/jb.181.24.7421-7429.1999

  90. 90.

    Chae KS Lee IH Choi CS Kim HR Purification and characterization of chitin-binding proteins from the hemolymph of sweet potato hornworm, Agrius convolvuliComp. Biochem. Physiol. B Biochem. Mol. Biol1999 124475481

    Not in our library10.1016/s0305-0491(99)00143-1

  91. 91.

    De Bolle MF David KM Rees SB Vanderleyden J Cammue BP Broekaert WF Cloning and characterization of a cDNA encoding an antimicrobial chitin-binding protein from amaranth, Amaranthus caudatusPlant Mol. Biol1993 2211871190

    Not in our library10.1007/bf00028991

  92. 92.

    Huang X Xie W Gong Z Characteristics and antifungal activity of a chitin binding protein from Ginkgo bilobaFEBS Lett2000 478123126

    Not in our library10.1016/s0014-5793(00)01834-2

  93. 93.

    Kolbe S Fischer S Becirevic A Hinz P Schrempf H The Streptomyces reticuli alpha-chitin-binding protein CHB2 and its geneMicrobiology1998 144Pt 512911297

    Not in our library10.1099/00221287-144-5-1291

  94. 94.

    Hamodrakas SJ Willis JH Iconomidou VA A structural model of the chitin-binding domain of cuticle proteinsInsect. Biochem. Mol. Biol2002 3215771583

    Not in our library10.1016/s0965-1748(02)00079-6

  95. 95.

    Willis JH Cuticular Proteins in Insects and CrustaceansAm. Zool1999 39600609

    Not in our library

  96. 96.

    Eijsink VG Vaaje-Kolstad G Varum KM Horn SJ Towards new enzymes for biofuels: lessons from chitinase researchTrends Biotechnol2008 26228235

    Not in our library10.1016/j.tibtech.2008.02.004

  97. 97.

    Vaaje-Kolstad G Horn SJ van Aalten DM Synstad B Eijsink VG The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradationJ. Biol. Chem2005 2802849228497

    Not in our library10.1074/jbc.m504468200

  98. 98.

    Endo T Koizumi S Large-scale production of oligosaccharides using engineered bacteriaCurr. Opin. Struct. Biol2000 10536541

    Not in our library10.1016/s0959-440x(00)00127-5

  99. 99.

    Cottaz S Samain E Genetic engineering of Escherichia coli for the production of NI,NII-diacetylchitobiose (chitinbiose) and its utilization as a primer for the synthesis of complex carbohydratesMetab. Eng2005 7311317

    Not in our library10.1016/j.ymben.2005.05.004

  100. 100.

    Samain E Drouillard S Heyraud A Driguez H Geremia RA Gram-scale synthesis of recombinant chitooligosaccharides in Escherichia coliCarbohydr. Res1997 3023542

    Not in our library10.1016/s0008-6215(97)00107-9

  101. 101.

    Samain E Chazalet V Geremia RA Production of O-acetylated and sulfated chitooligosaccharides by recombinant Escherichia coli strains harboring different combinations of nod genesJ. Biotechnol1999 723347

    Not in our library10.1016/s0168-1656(99)00048-6

  102. 102.

    van der Holst PP Schlaman HR Spaink HP Proteins involved in the production and perception of oligosaccharides in relation to plant and animal developmentCurr. Opin. Struct. Biol2001 11608616

    Not in our library10.1016/s0959-440x(00)00255-4

  103. 103.

    Amatayakul-Chantler S Ferguson MAJ Dwek RA Rademacher TW Parekh RB Crandall IE Newell PC Cell surface oligosaccharides on Dictyostelium during developmentJ. Cell Sci1975 99485495

    Not in our library

  104. 104.

    Varki A Marth J Oligosaccharides in vertebrate developmentSemin. Dev. Biol1995 6127138

    Not in our library

  105. 105.

    Bakkers J Semino CE Stroband H Kijne JW Robbins PW Spaink HP An important developmental role for oligosaccharides during early embryogenesis of cyprinid fishProc. Natl. Acad. Sci. USA1997 9479827986

    Not in our library10.1073/pnas.94.15.7982

  106. 106.

    Iglesias M Soler RM Ribera J Esquerda JE Comella JX The carbohydrate N-acetylglucosamine is involved in the guidance of neurites from chick ciliary ganglion neurons through the extracellular matrix of rat skeletal muscle fiberNeurosci. Lett1996 2078184

    Not in our library10.1016/0304-3940(96)12506-4

  107. 107.

    Wells L Whelan SA Hart GW O-GlcNAc: a regulatory post-translational modificationBiochem. Biophys. Res. Commun2003 302435441

    Not in our library10.1016/s0006-291x(03)00175-x

  108. 108.

    Hurtado-Guerrero R Dorfmueller HC van Aalten DM Molecular mechanisms of O-GlcNAcylationCurr. Opin. Struct. Biol2008 18551557

    Not in our library10.1016/j.sbi.2008.09.005

  109. 109.

    Hart GW Dynamic O-linked glycosylation of nuclear and cytoskeletal proteinsAnnu. Rev. Biochem1997 66315335

    Not in our library10.1146/annurev.biochem.66.1.315

  110. 110.

    Kang E-S Han D Park J Kwak TK Oh M-A Lee S-A Choi S Park ZY Kim Y Lee JW O-GlcNAc modulation at Akt1 Ser473 correlates with apoptosis of murine pancreatic [beta] cellsExp. Cell Res2008 31422382248

    Not in our library10.1016/j.yexcr.2008.04.014

  111. 111.

    Yanagisawa M Yu RK O-linked beta-N-acetylglucosaminylation in mouse embryonic neural precursor cellsJ. Neurosci. Res2009 8735353545

    Not in our library10.1002/jnr.22170

  112. 112.

    Lazarus BD Love DC Hanover JA O-GlcNAc cycling: Implications for neurodegenerative disordersInt. J. Biochem. Cell Biol2009 4121342146

    Not in our library10.1016/j.biocel.2009.03.008

  113. 113.

    Zeidan Q Hart GW The intersections between O-GlcNAcylation and phosphorylation: implications for multiple signaling pathwaysJ. Cell Sci2010 1231322

    Not in our library10.1242/jcs.053678

  114. 114.

    Zachara NE Hart GW Cell signaling, the essential role of O-GlcNAc!Biochim. Biophys. Acta2006 1761599617

    Not in our library10.1016/j.bbalip.2006.04.007

  115. 115.

    Tallent MK Varghis N Skorobogatko Y Hernandez-Cuebas L Whelan K Vocadlo DJ Vosseller K In Vivo Modulation of O-GlcNAc Levels Regulates Hippocampal Synaptic Plasticity through Interplay with PhosphorylationJ. Biol. Chem2009 284174181

    Not in our library10.1074/jbc.m807431200

  116. 116.

    Brimble S Wollaston-Hayden EE Teo CF Morris AC Wells L The Role of the O-GlcNAc Modification in Regulating Eukaryotic Gene ExpressionCurr. Signal Transd. Ther2010 51224

    Not in our library10.2174/157436210790226465

  117. 117.

    Comer FI Hart GW O-GlcNAc and the control of gene expressionBiochim. Biophys. Acta1999 1473161171

    Not in our library10.1016/s0304-4165(99)00176-2

  118. 118.

    Hart GW Housley MP Slawson C Cycling of O-linked [beta]-N-acetylglucosamine on nucleocytoplasmic proteinsNature2007 44610171022

    Not in our library10.1038/nature05815

  119. 119.

    Zachara NE Hart GW O-GlcNAc modification: a nutritional sensor that modulates proteasome functionTrends Cell Biol2004 14218221

    Not in our library10.1016/j.tcb.2004.03.005

  120. 120.

    Kang JG Park SY Ji S Jang I Park S Kim HS Kim SM Yook JI Park YI Roth J Cho JW O-GlcNAc protein modification in cancer cells increases in response to glucose deprivation through glycogen degradationJ. Biol. Chem2009 2843477734784

    Not in our library10.1074/jbc.m109.026351

  121. 121.

    Whelan SA Dias WB Thiruneelakantapillai L Lane MD Hart GW Regulation of insulin receptor substrate 1 (IRS-1)/AKT kinase-mediated insulin signaling by O-Linked beta-N-acetylglucosamine in 3T3-L1 adipocytesJ. Biol. Chem2010 28552045211

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