Novel Insights into Enzymatic Thermostability: The “Short Board” Theory and Zero‐Shot Hamiltonian Model
Sign Up to like & getrecommendations! Published in 2024 at "Advanced Science"
DOI: 10.1002/advs.202402441
Abstract: Understanding the mechanism underlying thermostabilization in naturally stable enzymes and enhancing the thermostability of unstable enzymes are crucial aspects in enzyme engineering. Despite the development of various engineering methods, there remains substantial scope for improvement.… read more here.
Keywords: thermostability; short board; model; board ... See more keywords
Enhancing thermostability by modifying flexible surface loops in an evolved high‐redox potential laccase
Sign Up to like & getrecommendations! 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
Improving thermostability of (R)‐selective amine transaminase from Aspergillus terreus through introduction of disulfide bonds
Sign Up to like & getrecommendations! 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
Characterization of maltose‐binding protein–fused heparinases with enhanced thermostability by application of rigid and flexible linkers
Sign Up to like & getrecommendations! Published in 2024 at "Biotechnology and Applied Biochemistry"
DOI: 10.1002/bab.2642
Abstract: Heparinases, including heparinases I–III (HepI, HepII, and HepIII, respectively), are important tools for producing low‐molecular‐weight heparin, an improved anticoagulant. The poor thermostability of heparinases significantly hinders their industrial and laboratory applications. To improve the thermostability… read more here.
Keywords: thermostability; linker; binding protein; mbp fused ... See more keywords
Dimerization of Proline Dehydrogenase from Thermus thermophilus Is Crucial for Its Thermostability.
Sign Up to like & getrecommendations! 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
Semi‐rational engineering of D‐allulose 3‐epimerase for simultaneously improving the catalytic activity and thermostability based on D‐allulose biosensor
Sign Up to like & getrecommendations! Published in 2024 at "Biotechnology Journal"
DOI: 10.1002/biot.202400280
Abstract: D‐Allulose is one of the most well‐known rare sugars widely used in food, cosmetics, and pharmaceutical industries. The most popular method for D‐allulose production is the conversion from D‐fructose catalyzed by D‐allulose 3‐epimerase (DAEase). To… read more here.
Keywords: thermostability; semi rational; engineering allulose; allulose epimerase ... See more keywords
Rational Design of an Epoxide Hydrolase From Spatholobus Suberectus: Enhancing Catalytic Activity and Thermostability for Efficient (R)‐Styrene Oxide Production
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DOI: 10.1002/biot.70061
Abstract: (R)‐Styrene oxide is a high‐value chiral intermediate in pharmaceutical and chemical industries, yet its enantioselective synthesis remains challenging. Here, we engineered an epoxide hydrolase from Spatholobus suberectus (SsEH) to address its limitations in catalytic activity… read more here.
Keywords: thermostability; epoxide hydrolase; catalytic activity; styrene oxide ... See more keywords
Computer‐directed rational design enhanced the thermostability of carbonyl reductase LsCR for the synthesis of ticagrelor precursor
Sign Up to like & getrecommendations! Published in 2024 at "Biotechnology and Bioengineering"
DOI: 10.1002/bit.28662
Abstract: Carbonyl reductases are useful for producing optically active alcohols from their corresponding prochiral ketones. Herein, we applied a computer‐assisted strategy to increase the thermostability of a previously constructed carbonyl reductase, LsCRM4 (N101D/A117G/F147L/E145A), which showed an… read more here.
Keywords: synthesis ticagrelor; computer; thermostability; carbonyl ... See more keywords
Rational design of disulfide bonds to increase thermostability of Rhodococcus opacus catechol 1,2 dioxygenase
Sign Up to like & getrecommendations! Published in 2024 at "Biotechnology and Bioengineering"
DOI: 10.1002/bit.28808
Abstract: Catechol 1,2 dioxygenase is a versatile enzyme with several potential applications. However, due to its low thermostability, its industrial potential is not being met. In this study, the thermostability of a mesophilic catechol 1,2 dioxygenase… read more here.
Keywords: rhodococcus opacus; design disulfide; thermostability; catechol dioxygenase ... See more keywords
Oxetane Monomers Based On the Powerful Explosive LLM-116: Improved Performance, Insensitivity, and Thermostability.
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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
Peptide backbone circularization enhances antifreeze protein thermostability
Sign Up to like & getrecommendations! 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