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PubMed1995

Purification and characterization of chitin deacetylase from Colletotrichum lindemuthianum.

Chitin deacetylase (EC 3.5.1.41), the enzyme that catalyzes the hydrolysis of acetamido groups of N-acetyl-D-glucosamine in chitin, has been purified to homogeneity from the culture filtrate of the fungus Colletotrichum lindemuthianum and further characterized. The enzyme is a glycoprotein, and its apparent molecular mass was determined to be approximately 150 kDa. The glycosylation pattern of the enzyme is consistent with a mixture of N-linked glycans including oligomannosidic hybrid and/or complex type, and its carbohydrate content is approximately 67% by weight. Chitin deacetylase is active on several chitinous substrates and chitin derivatives, is not considerably inhibited by carboxylic acids, especially acetic acid, and exhibits a remarkable thermostability. The enzyme requires at least two N-acetyl-D-glucosamine residues (chitobiose) for catalysis. When glycol chitin (a water-soluble chitin derivative) was used as substrate, the optimum temperature for enzyme activity was determined to be 50 degrees C, and the optimum pH was approximately 8.5.

Amidohydrolases↗
PubMed1994

Effect of chitin and chitosan on nutrient digestibility and plasma lipid concentrations in broiler chickens.

Broiler chickens were fed on a control diet based on maize and maize starch or diets containing chitin, or 94, 82 or 76% deacetylated chitin (chitosans) with different viscosities (360, 590 and 620 m Pa.s respectively) at an inclusion level of 30 g/kg. Animals had free access to feed and water for the whole experimental period. On days 10 and 18 of the experiment chickens given the control and chitin-containing diets weighed more, had consumed more feed and had lower feed conversion ratios (g feed/g weight gain) than chitosan-fed birds. Feeding of chitosan-containing diets generally reduced total plasma cholesterol and high-density-lipoprotein (HDL)-cholesterol concentrations and gave an increased HDL:total cholesterol ratio in comparison with chickens given the control and chitin-containing diets. However, no significant reductions in plasma triacylglycerol concentrations resulting from feeding of the chitosan-containing diets were observed. The reduction in total cholesterol concentration and increased HDL:total cholesterol ratio were probably caused by enhanced reverse cholesterol transport in response to intestinal losses of dietary fats. The suggestion that dietary fat absorption was impeded by the chitosans was strengthened by the observation that ileal fat digestibility was reduced by 26% in comparison with control and chitin-fed animals. In a plasma triacylglycerol response study on day 21, feeding of 94 and 76%-chitosan-containing diets generally reduced postprandial triacylglycerol concentrations compared with chickens given the chitin-containing diet. Duodenal digestibilities of nutrients amongst chickens given the chitin-containing diet were generally lower than those of control and chitosan-fed birds indicating decreased intestinal transit time. The reduced caecal short-chain fatty acid concentrations of chickens given chitosan diets compared with the control diet illustrates the antimicrobial nature of chitosan. The fact that the three chitosan-containing diets affected the registered variables similarly indicated that the level of inclusion of chitosans in the diet exceeded the level at which the effect of the different viscosities could be significant.

Animals↗
PubMed2003

Chitin--the undisputed biomolecule of great potential.

Of the truly abundant polysaccharides in Nature, only chitin has yet to find utilization in large quantity. Chitin is the second most abundant natural biopolymer derived from exoskeletons of crustaceans and also from cell walls of fungi and insects. Chitin is a linear beta 1,4-linked polymer of N-acetyl-D-glucosamine (GlcNAc), whereas chitosan, a copolymer of GlcNAc (approximately 20%) and glucosamine (GlcN, 80%) residues, is a product derived from de-N-acetylation of chitin in the presence of hot alkali. Chitosan is, in fact, a collective name representing a family of de-N-acetylated chitins deacetylated to different degrees. Both chitin/chitosan and their modified derivatives find extensive applications in medicine, agriculture, food, and non-food industries as well. They have emerged as a new class of physiological materials of highly sophisticated functions. Their application versatility is a great challenge to the scientific community and to industry. All these are the result of their versatile biological activity, excellent biocompatibility, and complete biodegradability in combination with low toxicity. Commercial availability of high-purity forms of chitin/chitosan and the continuous appearance of new types of chitin/chitosan derivatives with more and more useful and specific properties have led to an unlimited R&D efforts on this most versatile amino polysaccharide, chitin to find new applications, which are necessary to realize its full potential. Incidentally, this too has become an environmental priority. No doubt, chitin is surely an undisputed biomolecule of great potential.

Animals↗
PubMed1991

CAL1, a gene required for activity of chitin synthase 3 in Saccharomyces cerevisiae.

The CAL1 gene was cloned by complementation of the defect in Calcofluor-resistant calR1 mutants of Saccharomyces cerevisiae. Transformation of the mutants with a plasmid carrying the appropriate insert restored Calcofluor sensitivity, wild-type chitin levels and normal spore maturation. Southern blots using the DNA fragment as a probe showed hybridization to a single locus. Allelic tests indicated that the cloned gene corresponded to the calR1 locus. The DNA insert contains a single open-reading frame encoding a protein of 1,099 amino acids with a molecular mass of 124 kD. The predicted amino acid sequence shows several regions of homology with those of chitin synthases 1 and 2 from S. cerevisiae and chitin synthase 1 from Candida albicans. calR1 mutants have been found to be defective in chitin synthase 3, a trypsin-independent synthase. Transformation of the mutants with a plasmid carrying CAL1 restored chitin synthase 3 activity; however, overexpression of the enzyme was not achieved even with a high copy number plasmid. Since Calcofluor-resistance mutations different from calR1 also result in reduced levels of chitin synthase 3, it is postulated that the products of some of these CAL genes may be limiting for expression of the enzymatic activity. Disruption of the CAL1 gene was not lethal, indicating that chitin synthase 3 is not an essential enzyme for S. cerevisiae.

Amino Acid Sequence↗
PubMedDate not supplied

Cartilage-scaffold composites produced by bioresorbable beta-chitin sponge with cultured rabbit chondrocytes.

We newly produced bioresorbable beta-chitin sponge and used it as a scaffold for three-dimensional culture of chondrocytes. beta-Chitin was obtained from the pens of Loligo squid and the beta-chitin sponge was formed into a pillar shape. We produced cartilage-scaffold composites with a cartilage-like layer at the surface by culturing beta-chitin sponge-attached chondrocytes at the surface for 4 weeks. The mean DNA content at week 4 was 2.52-fold more than preculture DNA content. The mean concentration values of chondroitin sulfate and hydroxyproline continued to increase after week 2. Type II collagen and aggrecan genes were both found to be expressed during the experiment. Overall results of the biochemical analysis, along with histochemical and immunohistochemical findings and RT-PCR analysis, indicate that the cartilage-like layer in the chondrocyte-beta-chitin sponge composite was similar to hyaline cartilage. Electron microscopy scanning also revealed that the cell layer at the surface of the beta-chitin sponge was filled with chondrocytes and abundant extracellular matrix. beta-Chitin sponge can be considered biocompatible with chondrocytes, and an adequate scaffold for three-dimensional chondrocyte culture. Because this technique can produce a pillar-shaped composite, we will be able to press-fit the composites into articular cartilage defects without covering the periosteum or suturing the implant.

Animals↗
PubMed2004

Candida albicans mutants in the BNI4 gene have reduced cell-wall chitin and alterations in morphogenesis.

The Candida albicans BNI4 gene was identified by homology to the Saccharomyces cerevisiae orthologue and encodes a predicted 1655 amino acid protein. In S. cerevisiae most cell-wall chitin is associated with primary septum formation and Bni4p is involved in tethering the Chs3p chitin synthase enzyme to the mother-bud neck by forming a bridge between a regulatory protein Chs4p and the septin Cdc10p. CaBni4p shows 20 % overall identity to the ScBni4p, with 73 % identity over the C-terminal 63 amino acids, which includes a putative protein phosphatase type 1 (PP1) binding domain. Northern blot analysis revealed a transcript of the expected size that was expressed in both yeast and hyphal growth forms. C. albicans has more chitin in its cell wall than S. cerevisiae, and again most chitin is synthesized by CaChs3p. The function of CaBNI4 was investigated by performing a targeted gene disruption using the 'Ura-blaster' method to delete amino acids 1120-1611 that are essential for function. The resulting Cabni4Delta/Cabni4Delta null mutants formed lemon-shaped yeast cells and had a 30 % reduction in cell-wall chitin, reduced hyphal formation on solid serum-containing medium and increased sensitivity to SDS and increased resistance to Calcofluor White. The Cabni4Delta/Cabni4Delta null mutants were unaffected in chitin ring formation, but often exhibited displaced bud sites with more obvious but flattened birth scars. Therefore, unlike in S. cerevisiae, the Cabni4 mutant apparently alters chitin distribution throughout the cell wall and not exclusively at the bud-neck region.

Candida albicans↗
PubMed1991

Chitin synthase 1 plays a major role in cell wall biogenesis in Neurospora crassa.

In filamentous fungi, chitin is a structural component of morphologically distinct structures assembled during various phases of growth and development. To investigate the role of chitin synthase in cell wall biogenesis in Neurospora crassa, we cloned a chitin synthase structural gene and examined the consequences of its inactivation. Using degenerate oligonucleotide mixtures designed on the basis of conserved sequences of the Saccharomyces cerevisiae CHS1 and CHS2 polypeptides, a DNA fragment encoding a similar predicted amino acid sequence was amplified from N. crassa genomic DNA. This product was used to probe N. crassa libraries for a gene homologous to one of the yeast genes. Full-length genomic and partial cDNA clones were identified, isolated, and sequenced. The amino acid sequence deduced from a cloned 3.4-kb gene [designated chitin synthase 1 (chs-1)] was very similar to that of the S. cerevisiae CHS1 and CHS2 and the Candida albicans CHS1 polypeptides. Inactivation of the N. crassa chs-1 gene by repeat-induced point mutation produced slow-growing progeny that formed hyphae with morphologic abnormalities. The chs-1RIP phenotype was correlated with a significant reduction in chitin synthase activity. Calcofluor staining of the chs-1RIP strain cross-walls, residual chitin synthase activity, and the increased sensitivity of the chs-1RIP strain to Nikkomycin Z suggest that N. crassa produces additional chitin synthase that can participate in cell wall formation.

Amino Acid Sequence↗
PubMed2001

Binding site for chitin oligosaccharides in the soybean plasma membrane.

Affinity cross-linking of the plasma membrane fraction to an (125)I-labeled chitin oligosaccharide led to the identification and characterization of an 85-kD, chitin binding protein in plasma membrane-enriched fractions from both suspension-cultured soybean cells and root tissue. Inhibition analysis indicated a binding preference for larger (i.e. degrees of polymerization = 8) N-acetylated chitin molecules with a 50% inhibition of initial activity value of approximately 50 nM. N-Acetyl-glucosamine and chitobiose showed no inhibitory effects at concentrations as high as 250 microM. It is noteworthy that the major lipo-chitin oligosaccharide Nod signal produced by Bradyrhizobium japonicum was also shown to be a competitive inhibitor of ligand binding. However, the binding site appeared to recognize the chitin portion of the Nod signal, and it is unlikely that this binding activity represents a specific Nod signal receptor. Chitooligosaccharide specificity for induction of medium alkalinization and the generation of reactive oxygen in suspension-cultured cells paralleled the binding activity. Taken together, the presence of the chitin binding protein in the plasma membrane fraction and the specificity and induction of a biological response upon ligand binding suggest a role for the protein as an initial response mechanism for chitin perception in soybean (Glycine max).

Binding Sites↗
PubMed1984

Protecting effect of chitin and chitosan on experimentally induced murine candidiasis.

Chitin and chitosan were found to exhibit a protective effect on mice administered these polysaccharides intraperitoneally against infection of the viable cells of Candida albicans NIH A-207 strain. A significant difference was observed between the protective effects of chitin and chitosan, i.e., chitin was much more effective than chitosan when the C. albicans cells were challenged via the intravenous route. In intraperitoneal inoculations of C. albicans cells, however, chitosan provided stronger resistance for mice than chitin. It has also been revealed that the number of polymorphonuclear leukocytes from circulating blood of chitin-administered mice increased remarkably compared with that of untreated and chitosan-treated mice, and that the increase of active oxygen-generating phagocytic cells was significant. On the other hand, the number of peritoneal exudate cells (PEC) and the amounts of active oxygen generated from these cells in chitosan-treated mice were larger than those of chitin-treated mice. However, candidacidal activities of PEC per fixed cell number in mice treated with chitin or with chitosan were almost the same and greater than those of untreated mice.

Animals↗
PubMed2002

Identification and characterization of the gene cluster involved in chitin degradation in a marine bacterium, Alteromonas sp. strain O-7.

Alteromonas sp. strain O-7 secretes chitinase A (ChiA), chitinase B (ChiB), and chitinase C (ChiC) in the presence of chitin. A gene cluster involved in the chitinolytic system of the strain was cloned and sequenced upstream of and including the chiA gene. The gene cluster consisted of three different open reading frames organized in the order chiD, cbp1, and chiA. The chiD, cbp1, and chiA genes were closely linked and transcribed in the same direction. Sequence analysis indicated that Cbp1 (475 amino acids) was a chitin-binding protein composed of two discrete functional regions. ChiD (1,037 amino acids) showed sequence similarity to bacterial chitinases classified into family 18 of glycosyl hydrolases. The cbp1 and chiD genes were expressed in Escherichia coli, and the recombinant proteins were purified to homogeneity. The highest binding activities of Cbp1 and ChiD were observed when alpha-chitin was used as a substrate. Cbp1 and ChiD possessed a chitin-binding domain (ChtBD) belonging to ChtBD type 3. ChiD rapidly hydrolyzed chitin oligosaccharides in sizes from trimers to hexamers, but not chitin. However, after prolonged incubation with large amounts of ChiD, the enzyme produced a small amount of (GlcNAc)(2) from chitin. The optimum temperature and pH of ChiD were 50 degrees C and 7.0, respectively.

Alteromonas↗
PubMed1975

Timing and function of chitin synthesis in yeast.

A temperature-sensitive mutant of Saccharomyces cerevisiae, L-2-42, is blocked at 37 C at a stage of the cell cycle prior to septum formation. When single cells of the mutant are allowed to bud at 37 C in a medium containing tritiated glucose, a large incorporation of radioactivity into chitin takes place. Thus, the synthesis of chitin, the major component of the primary septum, is initiated in a phase of the cell cycle which precedes septum closure. This early period of chitin synthesis is not required for emergence and growth of buds because, in the wild type, budding takes place normally in the presence of concentrations of polyoxin D that effectively and specifically prevent chitin formation. However, at a later time a majority of these cells lyse, presumably because of the inability to form a septum. Polyoxin D also prevents the appearance of enhanced fluorescence at the junction between mother cell and bud, as observed in the presence of a brightener. Therefore, the fluorescence is due to chitin and its presence at the base of very early buds indicates that chitin synthesis begins at or shortly after bud emergence. A scheme for chitin synthesis and primary septum formation which embodies these and other results is presented.

Anti-Bacterial Agents↗
PubMed1990

Chitinase system of Bacillus circulans WL-12 and importance of chitinase A1 in chitin degradation.

Bacillus circulans WL-12, isolated as a yeast cell wall-lytic bacterium, secretes a variety of polysaccharide-degrading enzymes into culture medium. When chitinases of the bacterium were induced with chitin, six distinct chitinase molecules were detected in the culture supernatant. These chitinases (A1, A2, B1, B2, C, and D) showed the following distinct sizes and isoelectric points: Mr 74,000, pI 4.7 (A1); Mr 69,000, pI 4.5 (A2); Mr 38,000, pI 6.6 (B1); Mr 38,000, pI 5.9 (B2); Mr 39,000, pI 8.5 (C); and Mr 52,000, pI 5.2 (D). Among these chitinases, A1 and A2 had the highest colloidal-chitin-hydrolyzing activities. Chitinase A1 showed a strong affinity to insoluble substrate chitin. Purified chitinase A1 released predominantly chitobiose [(GlcNAc)2] and a trace amount of N-acetylglucosamine (GlcNAc) from colloidal chitin. N-terminal amino acid sequence analysis of chitinases A1 and A2 indicated that chitinase A2 was generated from chitinase A1, presumably by proteolytic removal of a C-terminal portion of chitinase A1. Since chitinase A2 did not have the ability to bind to chitin, the importance of the C-terminal region of chitinase A1 to the strong affinity of chitinase A1 to substrate chitin was suggested. Strong affinity of the chitinase seemed to be required for complete degradation of insoluble substrate chitin. From these results, it was concluded that chitinase A1 is the key enzyme in the chitinase system of this bacterium.

Amino Acid Sequence↗
PubMed1997

Cloning, sequencing, and expression of the gene encoding Clostridium paraputrificum chitinase ChiB and analysis of the functions of novel cadherin-like domains and a chitin-binding domain.

The Clostridium paraputrificum chiB gene, encoding chitinase B (ChiB), consists of an open reading frame of 2,493 nucleotides and encodes 831 amino acids with a deduced molecular weight of 90,020. The deduced ChiB is a modular enzyme composed of a family 18 catalytic domain responsible for chitinase activity, two reiterated domains of unknown function, and a chitin-binding domain (CBD). The reiterated domains are similar to the repeating units of cadherin proteins but not to fibronectin type III domains, and therefore they are referred to as cadherin-like domains. ChiB was purified from the periplasm fraction of Escherichia coli harboring the chiB gene. The molecular weight of the purified ChiB (87,000) by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis, was in good agreement with the value (86,578) calculated from the deduced amino acid sequence excluding the signal peptide. ChiB was active toward chitin from crab shells, colloidal chitin, glycol chitin, and 4-methylumbelliferyl beta-D-N,N'-diacetylchitobioside [4-MU-(GlcNAc)2]. The pH and temperature optima of the enzyme were 6.0 and 45 degrees C, respectively. The Km and Vmax values for 4-MU-(GlcNAc)2 were estimated to be 6.3 microM and 46 micromol/min/mg, respectively. SDS-PAGE, zymogram, and Western blot analyses using antiserum raised against purified ChiB suggested that ChiB was one of the major chitinase species in the culture supernatant of C. paraputrificum. Deletion analysis showed clearly that the CBD of ChiB plays an important role in hydrolysis of native chitin but not processed chitin such as colloidal chitin.

Amino Acid Sequence↗
PubMed2000

Identification of a chitin-binding protein secreted by Pseudomonas aeruginosa.

One of the major proteins secreted by Pseudomonas aeruginosa is a 43-kDa protein, which is cleaved by elastase into smaller fragments, including a 30-kDa and a 23-kDa fragment. The N-terminal 23-kDa fragment was previously suggested as corresponding to a staphylolytic protease and was designated LasD (S. Park and D. R. Galloway, Mol. Microbiol. 16:263-270, 1995). However, the sequence of the gene encoding this 43-kDa protein revealed that the N-terminal half of the protein is homologous to the chitin-binding proteins CHB1 of Streptomyces olivaceoviridis and CBP21 of Serratia marcescens and to the cellulose-binding protein p40 of Streptomyces halstedii. Furthermore, a short C-terminal fragment shows homology to a part of chitinase A of Vibrio harveyi. The full-length 43-kDa protein could bind chitin and was thereby protected against the proteolytic activity of elastase, whereas the degradation products did not bind chitin. The purified 43-kDa chitin-binding protein had no staphylolytic activity, and comparison of the enzymatic activities in the extracellular medium of a wild-type strain and a chitin-binding protein-deficient mutant indicated that the 43-kDa protein supports neither chitinolytic nor staphylolytic activity. We conclude that the 43-kDa protein, which was found to be produced by many clinical isolates of P. aeruginosa, is a chitin-binding protein, and we propose to name it CbpD (chitin-binding protein D).

Amino Acid Sequence↗
PubMed2002

Molecular analysis of the gene encoding a novel chitin-binding protease from Alteromonas sp. strain O-7 and its role in the chitinolytic system.

Alteromonas sp. strain O-7 secretes several proteins in response to chitin induction. We have found that one of these proteins, designated AprIV, is a novel chitin-binding protease involved in chitinolytic activity. The gene encoding AprIV (aprIV) was cloned in Escherichia coli. DNA sequencing analysis revealed that the open reading frame of aprIV encoded a protein of 547 amino acids with a calculated molecular mass of 57,104 Da. AprIV is a modular enzyme consisting of five domains: the signal sequence, the N-terminal proregion, the family A subtilase region, the polycystic kidney disease domain (PkdD), and the chitin-binding domain type 3 (ChtBD3). Expression plasmids coding for PkdD or both PkdD and ChtBD (PkdD-ChtBD) were constructed. The PkdD-ChtBD but not PkdD exhibited strong binding to alpha-chitin and beta-chitin. Western and Northern analyses demonstrated that aprIV was induced in the presence of N-acetylglucosamine, N-acetylchitobiose, or chitin. Native AprIV was purified to homogeneity from Alteromonas sp. strain O-7 and characterized. The molecular mass of mature AprIV was estimated to be 44 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The optimum pH and temperature of AprIV were pH 11.5 and 35 degrees C, respectively, and even at 10 degrees C the enzyme showed 25% of the maximum activity. Pretreatment of native chitin with AprIV significantly promoted chitinase activity.

Alteromonas↗
PubMed1978

Localization of chitin in algal and fungal cell walls by light and electron microscopy.

Chitin was visualized in cell walls after hydrolysis with potassium hydroxide and subsequent postfixation of the deacetylated polysaccharide (chitosan) in OsO4. Areas of chitin deposition appeared dark borwn by light microscopy and electron dense in the electron microscope. With this method, the presence of chitin was demonstrated in the cell walls of the green alga Pithophora oedogonia (Montagne) Wittrock and two fungi, Ceratocystis ulmi Buism. (C. Moreau) and Blastocladiella emersonii Cantino and Hyatt. Most of the chitin in P. oedogonia ws found in the crosswall disk and small amounts occurred in the outer longitudinal walls. The septal disk of C. ulmi also contained chitin, but significant amounts were present in the inner and outer regions of longitudinal walls as well. Chitin was present throughout the walls of B. emersonii. Small amounts of chitin were not easily demonstrated by this technique, but removal of chitosan by exposure to dilute acetic acid before osmium fixation disrupted cell wall integrity, suggesting that small amounts of the structural polysaccharide had been removed.

Ascomycota↗
PubMed2003

Carbohydrate binding specificity of the recombinant chitin-binding domain of human macrophage chitinase.

The chitin-binding domain of human macrophage chitinase was expressed as a fusion protein with glutathione S-transferase in Escherichia coli and assayed for its binding activity. The purified recombinant chitin-binding domain bound to chitin, but not to glucan, xylan, or mannan. The binding of the recombinant chitin-binding domain to chitin was inhibited by N-acetylglucosamine, di-N-acetylchitobiose, and hyaluronan, but not by N-acetylgalactosamine or chondroitin. Furthermore, a solid-phase binding assay showed that the recombinant domain interacts specifically with hyaluronan and hybrid-type N-linked oligosaccharide chains on glycoproteins, and that the oligosaccharide-binding characteristics are similar to those of wheat germ agglutinin, a lectin that binds to chitin. The results suggest that human chitinase chitin-binding domain may be involved in tissue remodeling through binding to polysaccharides or extracellular matrix glycoproteins, and this recombinant protein can be used to elucidate biological functions of the enzyme.

Base Sequence↗
PubMed1993

Polymeric N-acetyl-D-glucosamine (chitin) induces histionic activation in dogs.

Analyses on the effects of polymeric N-acetyl-D-glucosamine (chitin), which was obtained from squid pen, on histiogenic activation in dogs were carried out with subcutaneous implants (5 x 5 cm2) of polyester non-woven fabric (NWF) supplemented with chitin (chitin group) and NWF (control group). These materials were implanted at 4 sites, on the lumbodorsal and lumbosacral subcutaneous tissues on both sides of the midline in each dog under general anesthesia. The implants and their surrounding tissues were isolated on post-implantation days (PIDs) 2, 4, 8, and 18 under general anesthesia. In the chitin group, the implant was organized gradually and its organization was completed on PID 18, when obvious angiogenesis toward the NWF was observed. On the other hand, in the control group, obvious angiogenesis toward the NWF was not observed macroscopically. Numbers of mononuclear (MN) and polymorphonuclear (PMN) cells concentrated around the implants on PID 2 were larger in the chitin than control group. In the chitin group, formation of granulating tissue around the implant was indicated on PID 4, whereas such a phenomenon was not observed in the control group. From these results, chitin accelerates the migration of MN and PMN cells to the NWF site with rapid follow-up organization of the NWF accompanied by angiogenesis.

Animals↗