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Cloning, purification, and characterization of chitinase from Bacillus sp. DAU101 [An article from: Bioresource Technology]
Book Details
PublisherElsevier
ISBN / ASINB000PDYRVU
ISBN-13978B000PDYRV2
AvailabilityAvailable for download now
MarketplaceUnited States 🇺🇸
Description
This digital document is a journal article from Bioresource Technology, published by Elsevier in 2007. The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser.
Description:
A chitinase encoding gene from Bacillus sp. DAU101 was cloned in Escherichia coli. The nucleotide sequencing revealed a single open reading frame containing 1781 bp and encoding 597 amino acids with 66kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and zymogram. The chitinase was composed of three domains: a catalytic domain, a fibronectin III domain, and a chitin binding domain. The chitinase was purified by GST-fusion purification system. The pH and temperature optima of the enzyme were 7.5 and 60^oC, respectively. The metal ions, Zn^2^+, Cu^2^+, and Hg^2^+, were strongly inhibited chitinase activity. However, chitinase activity was increased 1.4-fold by Co^2^+. Chisb could hydrolyze GlcNAc"2 to N-acetylglucosamine and was produced GlcNAc"2, when chitin derivatives were used as the substrate. This indicated that Chisb was a bifunctional enzyme, N-acetylglucosaminase and chitobiosidase. The enzyme could not hydrolyze glycol chitin, glycol chitosan, or CMC, but hydrolyzed colloidal chitin and soluble chitosan.
Description:
A chitinase encoding gene from Bacillus sp. DAU101 was cloned in Escherichia coli. The nucleotide sequencing revealed a single open reading frame containing 1781 bp and encoding 597 amino acids with 66kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and zymogram. The chitinase was composed of three domains: a catalytic domain, a fibronectin III domain, and a chitin binding domain. The chitinase was purified by GST-fusion purification system. The pH and temperature optima of the enzyme were 7.5 and 60^oC, respectively. The metal ions, Zn^2^+, Cu^2^+, and Hg^2^+, were strongly inhibited chitinase activity. However, chitinase activity was increased 1.4-fold by Co^2^+. Chisb could hydrolyze GlcNAc"2 to N-acetylglucosamine and was produced GlcNAc"2, when chitin derivatives were used as the substrate. This indicated that Chisb was a bifunctional enzyme, N-acetylglucosaminase and chitobiosidase. The enzyme could not hydrolyze glycol chitin, glycol chitosan, or CMC, but hydrolyzed colloidal chitin and soluble chitosan.
