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 Biochemjournal_title
Journal of biochemistryauthors
Hara S,Yamamura Y,Fujii Y,Mega T,Ikenaka Tdoi
10.1093/oxfordjournals.jbchem.a122691subject
Has Abstractpub_date
1989-03-01 00:00:00pages
484-9issue
3eissn
0021-924Xissn
1756-2651journal_volume
105pub_type
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journal_title:Journal of biochemistry
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journal_title:Journal of biochemistry
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更新日期:1984-06-01 00:00:00
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pub_type: 杂志文章
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journal_title:Journal of biochemistry
pub_type: 杂志文章
doi:10.1093/oxfordjournals.jbchem.a123657
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pub_type: 杂志文章
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更新日期:1999-09-01 00:00:00
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pub_type: 杂志文章
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更新日期:1981-01-01 00:00:00
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pub_type: 杂志文章
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更新日期:1995-04-01 00:00:00
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pub_type: 杂志文章
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pub_type: 杂志文章
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更新日期:1996-01-01 00:00:00
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更新日期:2017-09-01 00:00:00