Active site directed chemical modification of α-galactosidase from Bacillus stearothermophilus (NCIM 5146): Involvement of lysine, tryptophan and carboxylate residues in catalytic site-Reference-Cited by-同舟云学术

Active site directed chemical modification of α-galactosidase from Bacillus stearothermophilus (NCIM 5146): Involvement of lysine, tryptophan and carboxylate residues in catalytic site

Published:2007-04 Issue:5 Volume:40 Page:1312-1320
ISSN:0141-0229
Container-title:Enzyme and Microbial Technology
language:en
Short-container-title:Enzyme and Microbial Technology

Author:

Gote M.M.,Khan M.I.,Khire J.M.

Publisher

Elsevier BV

Subject

Applied Microbiology and Biotechnology,Biochemistry,Biotechnology,Bioengineering

Reference38 articles.

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4. Soymilk oligosaccharide hydrolysis by Aspergillus oryzae α-galactosidase immobilized in calcium alginate;Prashanth;Process Biochem,2005

5. Purification and characterization of thermostable β-mannanase and α-galactosidase from Bacillus stearothermophilus;Talbot;Appl Environ Microbiol,1990

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