Unusual susceptibility of chitosan to enzymic hydrolysis

Pantaleone, David P.; Yalpani, Manssur; Scollar, Mark P.

doi:10.1016/s0008-6215(92)84256-r

Cited by 123 publications

(67 citation statements)

References 8 publications

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“…Since chitosanase, the enzyme for chitosanolysis, is expensive and unavailable in bulk, there was a need to identify an alternative and inexpensive way for obtaining chitosan depolymerization products. During search for the same, susceptibility of chitosan to various non-specific enzymes such as cellulase, pectinase, pepsin, papain and wheatgerm lipase was reported, although the enzyme purity was in doubt [10,11].…”

Section: Introductionmentioning

confidence: 99%

Characterization of chito-oligosaccharides prepared by chitosanolysis with the aid of papain and Pronase, and their bactericidal action against Bacillus cereus and Escherichia coli

Kumar

Varadaraj

Gowda

et al. 2005

Biochemical Journal

202

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Papain (from papaya latex; EC 3.4.22.2) and Pronase (from Streptomyces griseus; EC 3.4.24.31) caused optimum depolymerization of chitosan at pH 3.5 and 37• C, resulting in LMMC (low molecular mass chitosan) and chito-oligomeric-monomeric mixture. The yield of the latter was 14-16 % and 14-19 % respectively for papain-and Pronase-catalysed reactions, depending on the reaction time (1-5 h). HPLC revealed the presence of monomer(s) and oligomers of DP (degree of polymerization) 2-6, which was also confirmed by matrix-assisted laser-desorption ionization-time-of-flight MS. Along with the chito-oligomers, the appearance of only GlcNAc (N-acetylglucosamine) in Pronasecatalysed chitosanolysis was indicative of its different action pattern compared with papain. Fourier-transform infrared, liquidstate 13 C-NMR spectra and CD analyses of chito-oligomericmonomeric mixture indicated the release of GlcNAc/GlcNAc-rich oligomers. The monomeric sequence at the non-reducing ends of chito-oligomers was elucidated using N-acetylglucosaminidase. The chito-oligomeric-monomeric mixture showed better growth inhibitory activity towards Bacillus cereus and Escherichia coli compared with native chitosan. Optimum growth inhibition was observed with chito-oligomers of higher DP having low degree of acetylation. The latter caused pore formation and permeabilization of the cell wall of B. cereus, whereas blockage of nutrient flow due to the aggregation of chito-oligomers-monomers was responsible for the growth inhibition and lysis of E. coli, which were evidenced by scanning electron microscopy analysis. The spillage of cytoplasmic enzymes and native PAGE of the cellfree supernatant of B. cereus treated with chito-oligomeric-monomeric mixture further confirmed bactericidal activity of the latter. Use of papain and Pronase, which are inexpensive and easily available, for chitosanolysis, is of commercial importance, as the products released are of considerable biomedical value.

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Section: Introductionmentioning

confidence: 99%

Characterization of chito-oligosaccharides prepared by chitosanolysis with the aid of papain and Pronase, and their bactericidal action against Bacillus cereus and Escherichia coli

Kumar

Varadaraj

Gowda

et al. 2005

Biochemical Journal

202

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“…The solid-state CP-MAS 13 C-NMR and IR spectra indicated chitosan to have a b-conformation, as evidenced by the absence of splitting of signals corresponding to C3-C5 carbons (Fig. 1) and appearance of a single broad peak around 3371 cm (Fig.…”

Section: Characterization Of Chitosanmentioning

confidence: 93%

“…The molecular mass of the major product, LMWC, varied between 9.0 ± 0.5 kDa depending on the reaction time. Scanning electron microscopy of LMWC showed an approximately eightfold decrease in particle size and characterization by infrared spectroscopy, circular dichroism, X-ray diffractometry and 13 C-NMR revealed them to possess a lower degree of acetylation, hydration and crystallinity compared to chitosan. Chitosanolysis by pronase is an alternative and inexpensive methodtoproduceavarietyofchitosandegradationproducts that have wide and varied biofunctionalities.…”

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confidence: 99%

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Non‐specific depolymerization of chitosan by pronase and characterization of the resultant products

Kumar¹,

Gowda

Tharanathan³

2004

European Journal of Biochemistry

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Pronase (type XXV serine protease from Streptomyces griseus) efficiently depolymerizes chitosan, a linear bfi1,4-linked polysaccharide of 2-amino-deoxyglucose and 2-amino-2-N-acetylamino-D-glucose, to low-molecular weight chitosans (LMWC), chito-oligomers (degree of polymerization, 2-6) and monomer. The maximum depolymerization occurred at pH 3.5 and 37°C, and the reaction obeyed Michaelis-Menten kinetics with a K m of 5.21 mgAEmL )1 and V max of 138.55 nmolesAEmin. The molecular mass of the major product, LMWC, varied between 9.0 ± 0.5 kDa depending on the reaction time. Scanning electron microscopy of LMWC showed an approximately eightfold decrease in particle size and characterization by infrared spectroscopy, circular dichroism, X-ray diffractometry and 13 C-NMR revealed them to possess a lower degree of acetylation, hydration and crystallinity compared to chitosan. Chitosanolysis by pronase is an alternative and inexpensive methodtoproduceavarietyofchitosandegradationproducts that have wide and varied biofunctionalities.

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“…Structurally, it is considered a copolymer of glucosamine and N-acetylglucosamine units linked by β-1, 4 glycosidic bonds. It is a biodegradable material that can be decomposed under physiological conditions by lysozymes, proteinases and so on [17][18]. In the presence of enzyme, the amide bonds and glycosidic bonds in the chitosan can be slowly cut off.…”

Section: Introductionmentioning

confidence: 99%

Synthesis and characterization of temperature-sensitive and biodegradable hydrogel based on N-isopropylacrylamide

Zhu

et al. 2010

Open Chemistry

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Based on a biodegradable cross-linker, N-maleyl chitosan (N-MACH), a series of Poly(N-isopropylacrylamide) (PNIPAAm) and Poly(N-isopropylacrylamide-co-acrylamide) [P(NIPAAm-co-Am)] hydrogels were prepared, and their lower critical solution temperature (LCST), swelling kinetics, equilibrium swelling ratio in NaCl solution, and enzymatic degradation behavior in simulated gastric fluids (SGF) were discussed. The LCST did not change with different cross-linker contents. By altering the NIPAAm/Am molar ratio of P(NIPAAm-co-Am) hydrogels, the LCST could be increased to 39°C. The LCST of the hydrogel was significantly influenced by the monomer ratio of the NIPAAm/Am but not by the cross-linker content. In the swelling kinetics, all the dry hydrogels exhibited fast swelling behavior, and the swelling ratios were influenced by the cross-linker content and NIPAAm/Am molar ratios. Equilibrium swelling ratio of all the hydrogels decreased with increasing NaCl solution concentration. In enzymatic degradation tests, the weight loss of hydrogels was dependent on the cross-linker contents and the enzyme concentration. © Versita Sp. z o.o.

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Unusual susceptibility of chitosan to enzymic hydrolysis

Cited by 123 publications

References 8 publications

Characterization of chito-oligosaccharides prepared by chitosanolysis with the aid of papain and Pronase, and their bactericidal action against Bacillus cereus and Escherichia coli

Characterization of chito-oligosaccharides prepared by chitosanolysis with the aid of papain and Pronase, and their bactericidal action against Bacillus cereus and Escherichia coli

Non‐specific depolymerization of chitosan by pronase and characterization of the resultant products

Synthesis and characterization of temperature-sensitive and biodegradable hydrogel based on N-isopropylacrylamide

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