Random mutagenesis and disulfide bond formation improved thermostability in microbial transglutaminase
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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1 Online-Ressource.
- Language
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Englisch
- Bibliographic citation
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Random mutagenesis and disulfide bond formation improved thermostability in microbial transglutaminase ; volume:108 ; number:1 ; day:1 ; month:10 ; year:2024 ; pages:1-13 ; date:12.2024
Applied microbiology and biotechnology ; 108, Heft 1 (1.10.2024), 1-13, 12.2024
- Creator
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Suzuki, Mototaka
Date, Masayo
Kashiwagi, Tatsuki
Takahashi, Kazutoshi
Nakamura, Akira
Tanokura, Masaru
Suzuki, Eiichiro
Yokoyama, Keiichi
- Contributor
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SpringerLink (Online service)
- DOI
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10.1007/s00253-024-13304-1
- URN
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urn:nbn:de:101:1-2412182111136.796624556806
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:30 AM CEST
Data provider
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Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Suzuki, Mototaka
- Date, Masayo
- Kashiwagi, Tatsuki
- Takahashi, Kazutoshi
- Nakamura, Akira
- Tanokura, Masaru
- Suzuki, Eiichiro
- Yokoyama, Keiichi
- SpringerLink (Online service)
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Improving the thermostability of GH49 dextranase AoDex by site-directed mutagenesis
Improving the thermostability of alpha-amylase by combinatorial coevolving-site saturation mutagenesis
Engineered disulfide bonds improve thermostability and activity of L‐isoleucine hydroxylase for efficient 4‐HIL production in Bacillus subtilis 168
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Protein crystal quality oriented disulfide bond engineering
Electronic Synaptic Devices with High Thermostability Induced by Embedded Tungsten Disulfide Quantum Dots for Machine Learning
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Disulfide Bond Engineering of an Endoglucanase from Penicillium verruculosum to Improve Its Thermostability
Disulfide bond engineering of AppA phytase for increased thermostability requires co-expression of protein disulfide isomerase in Pichia pastoris
Improving the thermostability of GH49 dextranase AoDex by site-directed mutagenesis
Improving the thermostability of alpha-amylase by combinatorial coevolving-site saturation mutagenesis
Engineered disulfide bonds improve thermostability and activity of L‐isoleucine hydroxylase for efficient 4‐HIL production in Bacillus subtilis 168
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Electronic Synaptic Devices with High Thermostability Induced by Embedded Tungsten Disulfide Quantum Dots for Machine Learning