Chitin and chitosan can undergo nonspecific enzymatic hydrolysis by several different hydrolases. This susceptibility to nonspecific enzymes opens up many opportunities for producing chitooligosaccharides and low molecular weight chitopolysaccharides, since specific chitinases and chitosanases are rare and not commercially available. In this study, chitosan and chitin were hydrolyzed using several commercially available hydrolases. Among them, cellulases with the highest specific activity demonstrated the best activity, as indicated by the rapid decrease in viscosity of a chitosan solution. The hydrolysis of chitosan by nonspecific enzymes generated a sugar release that corresponded to the decrease in the degree of polymerization. This decrease reached a maximum of 3.3-fold upon hydrolysis of 10% of the sample. Cellulases were better than lysozyme or amylases at hydrolyzing chitosan and chitin. Analysis of 13C CP-MAS NMR and FTIR spectra of chitin after cellulase treatment revealed changes in the chitin crystal structure related to rearrangement of inter- and intramolecular H-bonds. The structural changes and decreases in crystallinity allowed dissolution of chitin molecules of high molecular weight and enhanced the solubility of chitin in alkali by 10-12% compared to untreated chitin.
Keywords: Cellulases; Cellulose-binding domain; Chitin; Chitosan; Crystalline structure.
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