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Improvement of the Thermal Stability of a Calcium-free, Alkaline α-Amylase by Site-directed Mutagenesis
Bacillus alkaliphile α-amylase thermostability site-directed mutagenesis
2008/4/20
Alkaline α-amylase from Bacillus sp. strain KSM-K38 (AmyK38) is a calcium-free enzyme that is stable against chelating and oxidative reagents. Recently, the thermostability of this enzyme was improved...
Production of Aldonic Acids from Monosaccharides by Washed Cells of Burkholderia cepacia and their Calcium Binding Capability
aldonic acid Burkholderia cepacia microbial conversion oxidation calcium binding
2008/4/20
Microbial oxidation of monosaccharides and calcium binding capability of the resulting aldonic acids were investigated. When washed cells of a strain of Burkholderia cepacia were shaken with 15% (w/v)...
An Oxidation Stable and Chelator-resistant, Calcium-free α-Amylase from the Alkaliphilic Bacillus Isolate KSM-K38
calcium-free α-amylase Bacillus oxidative stability chelator resistance
2008/4/20
We found a novel α-amylase (AmyK38) in a culture of a novel, alkaliphilic Bacillus sp. strain KSM-K38. The enzyme was an alkaline, liquefying α-amylase, having a pH optimum of 8.0-9.5, and exhibiting ...
Engineering Thermus Maltogenic Amylase with Improved Thermostability: Probing the Role of the Conserved Calcium Binding Site in Cyclodextrin-degrading Enzymes
calcium binding site cyclodextrin-degrading enzymes mutagenesis thermostability Thermus maltogenic amylase
2008/4/20
Thermus maltogenic amylase (ThMA), one of the cyclodextrin (CD)-degrading enzymes, is expected to have a calcium-binding site (Ca2 site) based on multiple sequence alignments. In spite of the presumpt...