Purification and characterization of chitinase produced by Streptomyces erythraeus.

Abstract:

:A chitinase was purified from the culture filtrate of Streptomyces erythraeus (SE). The enzyme (SE chitinase) has a molecular weight of 30,000 and pI 3.7, and shows optimal activity at pH 5.0 with an optimal ionic strength of less than 0.2 M NaCl. SE chitinase could hydrolyze chitin and its derivatives, but could not hydrolyze cell walls of Micrococcus lysodeikticus. The substrate specificity of SE chitinase was compared with those of hen egg white (HEW) and SE lysozymes. The binding mode of the chitinase to substrates was investigated using chitooligosaccharides and their derivatives. The results showed that the binding mode of SE chitinase to the substrate is similar to that of HEW and SE lysozymes.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Hara S,Yamamura Y,Fujii Y,Mega T,Ikenaka T

doi

10.1093/oxfordjournals.jbchem.a122691

subject

Has Abstract

pub_date

1989-03-01 00:00:00

pages

484-9

issue

3

eissn

0021-924X

issn

1756-2651

journal_volume

105

pub_type

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