A multi-factors rational design strategy for enhancing the thermostability of Escherichia coli AppA phytase. - Wikidata - awgldk - TriplyDB

A multi-factors rational design strategy for enhancing the thermostability of Escherichia coli AppA phytase.

A multi-factors rational design strategy for enhancing the thermostability of Escherichia coli AppA phytase.

http://www.wikidata.org/entity/Q51825100

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Defying the activity-stability trade-off in enzymes: taking advantage of entropy to enhance activity and thermostability.Improvement in the thermostability of a type A feruloyl esterase, AuFaeA, from Aspergillus usamii by iterative saturation mutagenesis.Amino-acid mutations to extend the biological half-life of a therapeutically valuable mutant of human butyrylcholinesterase.Biocatalysts: application and engineering for industrial purposes.Iterative key-residues interrogation of a phytase with thermostability increasing substitutions identified in directed evolution.Two strategies to engineer flexible loops for improved enzyme thermostability.Rational design of thermostability in bacterial 1,3-1,4-β-glucanases through spatial compartmentalization of mutational hotspots.Enhanced Thermostability of Lipoxygenase from Anabaena sp. PCC 7120 by Site-Directed Mutagenesis Based on Computer-Aided Rational Design.Current Progresses in Phytase Research: Three-Dimensional Structure and Protein Engineering

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P2860

A multi-factors rational design strategy for enhancing the thermostability of Escherichia coli AppA phytase.

http://www.wikidata.org/entity/Q51825100

description

2013 nî lūn-bûn

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2013年の論文

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2013年学术文章

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2013年学术文章

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2013年学术文章

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2013年学术文章

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2013年学术文章

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2013年学术文章

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2013年學術文章

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2013年學術文章

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name

A multi-factors rational desig ...... Escherichia coli AppA phytase.

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A multi-factors rational desig ...... Escherichia coli AppA phytase.

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type

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A multi-factors rational desig ...... Escherichia coli AppA phytase.

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A multi-factors rational desig ...... Escherichia coli AppA phytase.

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A multi-factors rational desig ...... Escherichia coli AppA phytase.

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A multi-factors rational desig ...... Escherichia coli AppA phytase.

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S10295-013-1260-Z

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Journal of Industrial Microbiology & Biotechnology

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A multi-factors rational desig ...... Escherichia coli AppA phytase

@en

P2093

Baojin Fei

http://www.w3.org/2001/XMLSchema#string

Dairong Qiao

http://www.w3.org/2001/XMLSchema#string

Hongxiu Guo

http://www.w3.org/2001/XMLSchema#string

Hui Xu

http://www.w3.org/2001/XMLSchema#string

Shuhan Ma

http://www.w3.org/2001/XMLSchema#string

Yi Cao

http://www.w3.org/2001/XMLSchema#string

Yu Cao

http://www.w3.org/2001/XMLSchema#string

P2860

Crystal structures of Escherichia coli phytase and its complex with phytate

Contribution of surface salt bridges to protein stability

Stabilizing Salt-Bridge Enhances Protein Thermostability by Reducing the Heat Capacity Change of Unfolding

The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures

Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability

Configurational entropy elucidates the role of salt-bridge networks in protein thermostability.

Core-directed protein design.

Knowledge-guided laboratory evolution of protein thermolability.

Modifying thermostability of appA from Escherichia coli.

Biotechnological production and applications of phytases.

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457-464

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10.1007/S10295-013-1260-Z

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5

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40

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