Enhancement of the thermostability and the catalytic efficiency of Bacillus pumilus CBS protease by site-directed mutagenesis.
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Current Technological Improvements in Enzymes toward Their Biotechnological Applications.Biochemical and molecular characterization of a serine keratinase from Brevibacillus brevis US575 with promising keratin-biodegradation and hide-dehairing activitiesProbing the crucial role of Leu31 and Thr33 of the Bacillus pumilus CBS alkaline protease in substrate recognition and enzymatic depilation of animal hideRational Engineering of a Cold-Adapted α-Amylase from the Antarctic Ciliate Euplotes focardii for Simultaneous Improvement of Thermostability and Catalytic Activity.Directed evolution improves the fibrinolytic activity of nattokinase from Bacillus natto.Increasing activity and thermal resistance of Bacillus gibsonii alkaline protease (BgAP) by directed evolution.Purification and biochemical characterization of two detergent-stable serine alkaline proteases from Streptomyces sp. strain AH4.Biocatalysts: application and engineering for industrial purposes.Mutagenesis and characterization of a Bacillus amyloliquefaciens strain for Cinnamomum camphora seed kernel oil extraction by aqueous enzymatic method.Single amino acid mutation alters thermostability of the alkaline protease from Bacillus pumilus: thermodynamics and temperature dependence.An Alkaline Protease from Bacillus pumilus MP 27: Functional Analysis of Its Binding Model toward Its Applications As Detergent Additive.Comparison of the structural basis for thermal stability between archaeal and bacterial proteins.An overview of Bacillus proteases: from production to application.Enhanced thermostability of keratinase by computational design and empirical mutation.Single-site substitutions improve cold activity and increase thermostability of the dehairing alkaline protease (DHAP).Engineering Bacillus pumilus alkaline serine protease to increase its low-temperature proteolytic activity by directed evolution.
P2860
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P2860
Enhancement of the thermostability and the catalytic efficiency of Bacillus pumilus CBS protease by site-directed mutagenesis.
description
2010 nî lūn-bûn
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2010年の論文
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2010年学术文章
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2010年学术文章
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2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
@zh-sg
2010年學術文章
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2010年學術文章
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name
Enhancement of the thermostabi ...... by site-directed mutagenesis.
@en
Enhancement of the thermostabi ...... by site-directed mutagenesis.
@nl
type
label
Enhancement of the thermostabi ...... by site-directed mutagenesis.
@en
Enhancement of the thermostabi ...... by site-directed mutagenesis.
@nl
prefLabel
Enhancement of the thermostabi ...... by site-directed mutagenesis.
@en
Enhancement of the thermostabi ...... by site-directed mutagenesis.
@nl
P2093
P1433
P1476
Enhancement of the thermostabi ...... by site-directed mutagenesis.
@en
P2093
Bassem Jaouadi
Richard Haser
Samir Bejar
P304
P356
10.1016/J.BIOCHI.2010.01.008
P577
2010-01-21T00:00:00Z