Purification and biochemical characterization of a novel transglutaminase from Mythimna separata larvae (Noctuidae, Lepidoptera)

Zhang, Lei; Rao, Wenbing; Muhayimana, Solange; Zhang, Xianfei; Xu, Jiuyong; Xiao, Ciying; Huang, Qingchun

doi:10.1016/j.jbiotec.2017.10.018

Cited by 5 publications

(4 citation statements)

References 34 publications

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“…[29][30][31] Despite the fact that some researchers have attempted to improve the catalytic activity and thermostability of enzymes through rational design, the requirements of industrialization are still not met. 32,33 In this study, three variants (Mut1: S2P-S23V-Y24N-R215A-K294L, Mut2:S2P-S23V-Y24N-R215A-H289Y, Mut3: S23V-Y24N-R215A-K269D-H289Y) with higher specific enzyme activity and thermostability were constructed based on the structure of MTG-WT. Among of variants, Mut2 had the highest specific enzyme activity (39.3 ± 1.6 U/mg) and thermostability (t 1/2 (60 • C) = 27.6 min), which were 2.4 and 10.2 times of those of MTG-WT, respectively.…”

Section: Discussionmentioning

confidence: 99%

“…Rapid and effective improvement of enzyme catalytic activity through reasonable design has always been a hot topic in the field of protein engineering, which not only provides excellent new enzyme sources to industrial production, but also helps to analyze the relationship between protein structure and properties 29–31 . Despite the fact that some researchers have attempted to improve the catalytic activity and thermostability of enzymes through rational design, the requirements of industrialization are still not met 32,33 …”

Section: Discussionmentioning

confidence: 99%

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Construction, expression, purification, characterization, and structural analysis of microbial transglutaminase variants

Song

Sheng

Zhou

et al. 2022

Biotech and App Biochem

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Microbial transglutaminase (MTG, EC 2.3.2.13) derived from Streptomyces mobaraensis is widely used in the food and pharmaceutical industry because of its ability to synthesize isopeptide bonds between the proteinogenic side chains of glutamine and lysine. The half-life (t 1/2 ) of the activated wild-type enzyme at 60 • C is 2 min. To improve the activity and thermostability of MTG for higher temperature application, three variants (Mut1, Mut2, and Mut3) were obtained by combining key amino acid mutations on the basis of previous research results.The best variant Mut2 with a specific combination of five of seven substitutions (S2P-S23V-Y24N-R215A-H289Y) shows a 10-fold increased half-life at 60 • C (t 1/2 = 27.6 min), and a 2.4-fold increased specific enzyme activity (39.3 U/mg). As measured by circular dichroism, the curve of Mut2 was basically the same as that of MTG-WT. The structural simulation of Mut2 shows that the overall structure is discoid with a crack, but the crack openings are wider than that of MTG-WT. Furthermore, structural analysis of Mut2 showed that there were seven hydrogen bonds and one π-anion interaction between Mut2 and its adjacent amino acids, and the number of hydrogen bonds was one more than that of MTG-WT (six hydrogen bonds).

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Construction, expression, purification, characterization, and structural analysis of microbial transglutaminase variants

Song

Sheng

Zhou

et al. 2022

Biotech and App Biochem

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“…The application of enzyme technology in the field of traditional food protein has great potential development (Yi, Zhang, & Wang, 2014; Zhang, Rao, Muhayimana, Zhang, & Huang, 2017). The development trend of food in the future is to improve the nutrition, texture, and flavor of food by biological enzyme preparation.…”

Section: Discussionmentioning

confidence: 99%

Cloning and expression of maize transglutaminase gene inEscherichia coliand its action over dairy proteins

Han

Qin

et al. 2020

J. Food Process. Preserv.

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“…For this reason is was separated and purified; MsTGase was obtained chromatographically by the precipitation of Sephadex G-100 gel and DEAE-C-52 ion-exchange column with 48-fold purification and a reproducible yield of approximately 12%. 47 It is known the ability of E. coli isolates to produce alkaline phosphatase enzyme (ALP). ALP can be extracted; the crude extract activity and specific activity was 1.86 unit/ml and 20.44 unit/mg protein, respectively.…”

confidence: 99%

Diethylaminoethyl cellulose (DEAE-C) between chromatography and synthetic applications

Aljaf¹,

Amin²,

Hussain³

et al. 2020

Arkivoc

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The aim of this review is to point out the attention of the reader to the use of DEAE-C in organic reactions, possibly not only devoted to the preparation of heterocycles but potentially extending to other classes of organic compounds. Being DEAE-C an ammonium salt commonly used in chromatographic applications, it can be considered as a potential mild acid catalyst or a proton donor and these features can in theory catalyze standard acid-catalyzed organic reactions. In addition, the resin nature of DEAE-C could suggest the way to perform organic reactions in the solid state.

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Purification and biochemical characterization of a novel transglutaminase from Mythimna separata larvae (Noctuidae, Lepidoptera)

Cited by 5 publications

References 34 publications

Construction, expression, purification, characterization, and structural analysis of microbial transglutaminase variants

Construction, expression, purification, characterization, and structural analysis of microbial transglutaminase variants

Cloning and expression of maize transglutaminase gene inEscherichia coliand its action over dairy proteins

Diethylaminoethyl cellulose (DEAE-C) between chromatography and synthetic applications

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