Improving the Thermostability and Catalytic Activity of an Inulosucrase by Rational Engineering for the Biosynthesis of Microbial Inulin.
Sign Up to like & getrecommendations! Published in 2021 at "Journal of agricultural and food chemistry"
DOI: 10.1021/acs.jafc.1c04852
Abstract: Thermostability and enzymatic activity are two vital indexes determining the application of an enzyme on an industrial scale. A truncated inulosucrase, Laga-ISΔ138-702, from Lactobacillus gasseri showed high catalysis activity. To further enhance its thermostability and… read more here.
Keywords: improving thermostability; thermostability catalytic; thermostability; activity inulosucrase ... See more keywords
Inside Out Computational Redesign of Cavities for Improving Thermostability and Catalytic Activity of Rhizomucor Miehei Lipase
Sign Up to like & getrecommendations! Published in 2023 at "Applied and Environmental Microbiology"
DOI: 10.1128/aem.02172-22
Abstract: In the present study, R. miehei lipase, which is widely used in various industries, provides an opportunity to explore the effects of internal cavities on the thermostability and catalytic activity of enzymes. Here, we execute… read more here.
Keywords: thermostability catalytic; internal cavities; catalytic activity; activity ... See more keywords
Molecular role of NAA38 in thermostability and catalytic activity of the human NatC N-terminal acetyltransferase.
Sign Up to like & getrecommendations! Published in 2022 at "Structure"
DOI: 10.2139/ssrn.4126600
Abstract: N-terminal acetylation occurs on over 80% of human proteins and is catalyzed by a family of N-terminal acetyltransferases (NATs). All NATs contain a small catalytic subunit, while some also contain a large auxiliary subunit that… read more here.
Keywords: naa38 thermostability; thermostability catalytic; role naa38; molecular role ... See more keywords