Articles with "thermostability" as a keyword



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Enhancing thermostability by modifying flexible surface loops in an evolved high‐redox potential laccase

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Published in 2019 at "AIChE Journal"

DOI: 10.1002/aic.16747

Abstract: High-redox potential laccases (HRPLs) from white-rot fungi are versatile biocatalysts whose practical use is highly dependent on their thermostability. In this work, an evolved HRPL variant was subjected to structure-guided evolution to improve its thermostability.… read more here.

Keywords: high redox; thermostability; surface; surface loops ... See more keywords
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Improving thermostability of (R)‐selective amine transaminase from Aspergillus terreus through introduction of disulfide bonds

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Published in 2018 at "Biotechnology and Applied Biochemistry"

DOI: 10.1002/bab.1572

Abstract: To improve the thermostability of (R)‐selective amine transaminase from Aspergillus terreus (AT‐ATA), we used computer software Disulfide by Design and Modelling of Disulfide Bonds in Proteins to identify mutation sites where the disulfide bonds were… read more here.

Keywords: selective amine; disulfide bonds; thermostability; amine transaminase ... See more keywords

Dimerization of Proline Dehydrogenase from Thermus thermophilus Is Crucial for Its Thermostability.

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Published in 2019 at "Biotechnology journal"

DOI: 10.1002/biot.201800540

Abstract: Thermus thermophilus proline dehydrogenase ( TtProDH) catalyzes the first step in proline catabolism. The thermostable flavoenzyme consists of a distorted triosephosphate isomerase (TIM) barrel and three N-terminal helices: αA, αB, and αC. Using maltose-binding protein… read more here.

Keywords: proline dehydrogenase; dimerization; thermostability; thermus ... See more keywords
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Oxetane Monomers Based On the Powerful Explosive LLM-116: Improved Performance, Insensitivity, and Thermostability.

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Published in 2022 at "ChemPlusChem"

DOI: 10.1002/cplu.202200049

Abstract: 3-Bromomethyl-3-hydroxymethyloxetane represents an inexpensive and versatile precursor for the synthesis of 3,3-disubstituted oxetane derivatives. In the present work, its synthesis was improved and energetic oxetanes based on the explosive LLM-116 (4-amino-3,5-dinitro-1H-pyrazole) prepared. Reaching detonation velocities… read more here.

Keywords: explosive llm; insensitivity; llm; llm 116 ... See more keywords
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Peptide backbone circularization enhances antifreeze protein thermostability

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Published in 2017 at "Protein Science"

DOI: 10.1002/pro.3228

Abstract: Antifreeze proteins (AFPs) are a class of ice‐binding proteins that promote survival of a variety of cold‐adapted organisms by decreasing the freezing temperature of bodily fluids. A growing number of biomedical, agricultural, and commercial products,… read more here.

Keywords: protein; thermostability; backbone circularization; afp ... See more keywords
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Ile258Met mutation of Brucella melitensis 7α-hydroxysteroid dehydrogenase significantly enhances catalytic efficiency, cofactor affinity, and thermostability.

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Published in 2021 at "Applied microbiology and biotechnology"

DOI: 10.1007/s00253-021-11299-7

Abstract: NAD(H)-dependent 7α-hydroxysteroid dehydrogenase catalyzes the oxidation of chenodeoxycholic acid to 7-oxolithocholic acid. Here, we designed mutations of Ile258 adjacent to the catalytic pocket of Brucella melitensis 7α-hydroxysteroid dehydrogenase. The I258M variant gave a 4.7-fold higher… read more here.

Keywords: catalytic efficiency; hydroxysteroid dehydrogenase; thermostability; mutation ... See more keywords
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Significantly improving the thermostability of a hyperthermophilic GH10 family xylanase XynAF1 by semi-rational design.

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Published in 2021 at "Applied microbiology and biotechnology"

DOI: 10.1007/s00253-021-11340-9

Abstract: Xylanases have a broad range of applications in industrial biotechnologies, which require the enzymes to resist the high-temperature environments. The majority of xylanases have maximum activity at moderate temperatures, which limited their potential applications in… read more here.

Keywords: family xylanase; xylanase; thermostability; gh10 family ... See more keywords
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Improving the thermostability of a GH97 dextran glucosidase by rational design

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Published in 2020 at "Biotechnology Letters"

DOI: 10.1007/s10529-020-02928-8

Abstract: This study was aimed at improving the thermostability of dextran glucosidase PspAG97A, a member of the glycoside hydrolase family 97, from Pseudoalteromonas sp. K8. A total of 9 lysine residues were chosen using the TKSA-MC… read more here.

Keywords: k75e k363e; improving thermostability; thermostability; charge ... See more keywords
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Critical effect of proline on thermostability of endoglucanase II from Penicillium verruculosum

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Published in 2019 at "Biochemical Engineering Journal"

DOI: 10.1016/j.bej.2019.107395

Abstract: Abstract Thermostability is an important protein property essential for the protein industrial application. Different approaches of rational design are used for protein thermostability improvement. In this research, the effect of proline substitutions on the protein… read more here.

Keywords: critical effect; effect proline; thermostability; effect ... See more keywords
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Thermostability detection and optimization of glycoengineered antibodies and antibody-drug conjugates based on differential scanning flouremitry analysis.

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Published in 2019 at "Bioorganic chemistry"

DOI: 10.1016/j.bioorg.2019.103391

Abstract: Thermostability of monoclonal antibodies (mAbs) and antibody-drug conjugates (ADCs), as a critical property of biotherapeutics, is important for their physicochemical processes, pharmacodynamics, and pharmacokinetics. Fc glycosylation of mAbs plays a crucial role in antibody functions… read more here.

Keywords: drug conjugates; differential scanning; analysis; thermostability ... See more keywords
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Disulfide bridge formation to increase thermostability of DFPase enzyme: A computational study

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Published in 2018 at "Computational biology and chemistry"

DOI: 10.1016/j.compbiolchem.2018.09.005

Abstract: Organophosphate compounds bioremediation by use of organophosphorus degradation enzymes such as DFPase is a developing interest in industry and medicine. The most important problem with the bio-catalytic enzymes is their instability on high temperatures. This… read more here.

Keywords: thermostability; bridge formation; dfpase enzyme; disulfide bridge ... See more keywords