Literature DB >> 12754823

[Effect of the degree of acetylation of chitosan on its enzymatic hydrolysis with the preparation Celloviridin G20x].

A V Il'ina1, V P Varlamov.   

Abstract

The degree of acetylation exerted only insignificant effects on the enzymatic hydrolysis of chitosan, while affecting the composition of the resulting hydrolysates and their water solubility. Chitosan with various degrees of acetylation was produced by reacetylation of the original chitosan (the solvents, methanol and 2% acetic acid, were present at a ratio of 54:51 v/v; the amount of acetic anhydride was in the range 0.1-2.0 mmol per 1 g chitosan). Hydrolysis by the enzymatic preparation Celloviridin G20x was performed at the enzyme to substrate ratio of 1:400 in sodium-acetate buffer, pH 5.2 (55 degrees C) for 1 h.

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Year:  2003        PMID: 12754823

Source DB:  PubMed          Journal:  Prikl Biokhim Mikrobiol        ISSN: 0555-1099


  1 in total

1.  A highly conserved arginine residue of the chitosanase from Streptomyces sp. N174 is involved both in catalysis and substrate binding.

Authors:  Marie-Ève Lacombe-Harvey; Mélanie Fortin; Takayuki Ohnuma; Tamo Fukamizo; Thomas Letzel; Ryszard Brzezinski
Journal:  BMC Biochem       Date:  2013-09-16       Impact factor: 4.059

  1 in total

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