Results 31 to 40 of about 26,595 (166)
Frontiers in Bioengineering and Biotechnology, 2022 In order to improve enzymatic properties of glucoamylases, six recombinant genes GA1–GA6 were created by domain shuffling of glucoamylase genes GAA1 from Aspergillus niger Ld418AI and GATE from Talaromyces emersonii Ld418 TE using overlap extension PCR ...
Zhongxiu Chen +15 more
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Microorganisms, 2021 This study analyzed the thermostability and effect of calcium ions on the enzymatic activity of α-amylase produced by Bacillus licheniformis strain LB04 isolated from Espinazo Hot springs in Nuevo Leon, Mexico. The enzyme was immobilized by entrapment on
Anaid Silva-Salinas +5 more
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Overproduction of Tk-Subtilisin and Elucidation of Its Structural Thermostability Based on Molecular Dynamics Studies [PDF]
Brazilian Archives of Biology and TechnologyBackground: Subtilisin from Thermococcus kodakaraensis (Tk-subtilisin) is an ideal candidate for many industrial and research processes due to its unique features. Methods: In this study, the enzyme is overproduced in E.
Nouman Rasool, Naeem Rashid
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Thermostable and Long-Circulating Albumin-Conjugated Arthrobacter globiformis Urate Oxidase
Pharmaceutics, 2021 Urate oxidase derived from Aspergillus flavus has been investigated as a treatment for tumor lysis syndrome, hyperuricemia, and gout. However, its long-term use is limited owing to potential immunogenicity, low thermostability, and short circulation time
Byungseop Yang, Inchan Kwon
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Parallel Strategy Increases the Thermostability and Activity of Glutamate Decarboxylase
Molecules, 2020 Glutamate decarboxylase (GAD; EC 4.1.1.15) is a unique pyridoxal 5-phosphate (PLP)-dependent enzyme that specifically catalyzes the decarboxylation of L-glutamic acid to produce γ-aminobutyric acid (GABA), which exhibits several well-known ...
Qing-Fei Zhang +5 more
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Foods, 2023 Proteases have been widely employed in many industrial processes. In this work, we aimed to improve the thermostability of the serine protease PB92 from Bacillus alcalophilus to meet the high-temperature requirements of biotechnological treatments. Eight
Huabiao Miao +4 more
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Understanding Thermostability Factors of Barley Limit Dextrinase by Molecular Dynamics Simulations
Frontiers in Molecular Biosciences, 2020 Limit dextrinase (LD) is the only endogenous starch-debranching enzyme in barley (Hordeum vulgare, Hv), which is the key factor affecting the production of a high degree of fermentation.
Juan Du +7 more
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Cryo-EM structure of a thermostable bacterial nanocompartment
IUCrJ, 2021 Protein nanocompartments are widespread in bacteria and archaea, but their functions are not yet well understood. Here, the cryo-EM structure of a nanocompartment from the thermophilic bacterium Thermotoga maritima is reported at 2.0 Å resolution.
Timothy Wiryaman, Navtej Toor
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Biology, 2021 l-asparaginase (EC 3.5.1.1) hydrolyzes l-asparagine to produce l-aspartate and ammonia and is widely found in microorganisms, plants, and some rodent sera. l-asparaginase used for industrial production should have good thermostability.
Xian Zhang +8 more
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Advanced ScienceUnderstanding the mechanism underlying thermostabilization in naturally stable enzymes and enhancing the thermostability of unstable enzymes are crucial aspects in enzyme engineering.
Min Liao +9 more
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