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Improvement of the Enzymatic Properties of Kojibiose Phosphorylase from Thermoanaerobacter brockii by Random Mutagenesis and Chimerization
kojibiose phosphorylase random mutagenesis chimerization Thermoanaerobacter brockii
2008/4/20
Random mutagenesis by error-prone PCR was introduced to kojibiose phosphorylase (KP; EC 2.4.1.230) from Thermoanaerobacter brockii ATCC35047. One thermostable mutant and two DP-mutants that were defin...
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...
Creation of a Novel Hydrolase by Site-directed Mutagenesis of Malto-oligosyltrehalose Synthase
trehalose malto-oligosyltrehalose synthase site-directed mutagenesis transglycosylation hydrolysis
2008/4/20
Malto-oligosyltrehalose synthase (EC 5.4.99.15, MTSase) catalyzes the conversion of α-1,4-glucan to glycosyltrehalose by forming an α,α-1,1-glucosidic linkage on the reducing side of the α-1,4-glucan....
Enhancing the Thermal Stability of Sucrose Phosphorylase from Streptococcus mutans by Random Mutagenesis
sucrose phosphorylase Streptococcus mutans random mutagenesis thermostable enzyme
2008/4/20
The thermal stability of sucrose phosphorylase (EC 2.4.1.7) from Streptococcus mutans was enhanced using random and site-directed mutageneses. Random mutagenesis studies revealed that eight single ami...
Mutagenesis and Structural Analysis of Thermoactinomyces vulgaris R-47 α-Amylase II (TVA II)
TVA II subsite substrate recognition α-amylase family
2008/4/20
An α-amylase II (TVA II) produced by Thermoactinomyces vulgaris R-47 exhibits wide substrate specificity for starch, pullulan, cyclodextrins and isopanose. Asp465 and Arg469 are located at subsite (-2...
Site-Directed Mutagenesis of Tryptophan 622 of Thermoactinomyces vulgaris R-47 Glucoamylase:pH Optima and Activities of Five Mutants
glucoamylase optimal pH catalytic base
2008/4/20
In Aspergillus awamori glucoamylase, the optimal pH has been reported to increase to maintain activity by a mutation of Ser411 which forms a hydrogen-bond with a catalytic base (Fang and Ford, Protein...