Properties of a novel thermostable glucose isomerase mined from Thermus oshimai and its application to preparation of high fructose corn syrup

Jia, Dong‐Xu; Zhou, Lin; Zheng, Yu‐Guo

doi:10.1016/j.enzmictec.2017.01.001

Cited by 52 publications

(22 citation statements)

References 28 publications

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“…Although this phenomenon is unusual, it was also observed in isomerization reaction catalyzed by natural enzyme Thermus oshimai (ToGI). [32] Then the yield and selectivity of fructose decreased rapidly with increasing pH.…”

Section: Effect Of Phmentioning

confidence: 99%

“…Natural glucose isomerases generally exhibit the best catalytic activity in weak alkaline solution, with the optimal pH of 7 to 9. [32,33] In order to achieve high conversion of glucose, the nonenzymatic isomerizations of glucose to fructose were usually carried out under acidic or alkaline conditions. However the selectivity of fructose was low.…”

Section: Effect Of Phmentioning

confidence: 99%

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Highly Selective Isomerization of Glucose into Fructose Catalyzed by a Mimic Glucose Isomerase

Zhang

Meng

et al. 2019

ChemCatChem

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An amphoteric phenolic compound with carboxyl and amino functional groups was synthesized and used as mimic glucose isomerase to catalyze the isomerization of glucose into fructose. The mimic enzyme displayed excellent catalytic activity for isomerization of glucose to fructose under mild conditions. The yield of fructose and selectivity of fructose could reach 33.0 % and 93.5 % after reacting 4 h, respectively, at pH 8.5 and 80°C. The catalysis reaction rate constant k cat and Michaelis constants K mG , K mF were calculated. The activation energy of glucose to fructose was evaluated as 65.9 kJ mol À 1 . The possible catalysis reaction mechanism was proposed. The acid-base groups on the catalyst play an important role in proton extraction and transfer, as well as in the rotation of local carbon chain, which leads to the highly selective isomerization of glucose into fructose under mild conditions.

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Section: Effect Of Phmentioning

confidence: 99%

Section: Effect Of Phmentioning

confidence: 99%

Highly Selective Isomerization of Glucose into Fructose Catalyzed by a Mimic Glucose Isomerase

Zhang

Meng

et al. 2019

ChemCatChem

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show abstract

“…There are several prokaryotic microorganism hosts used for production of recombinant proteins, including Escherichia coli and Bacillus subtilis [1,2]. E. coli, as one of hosts commonly used for recombinant protein expression, have many beneficial characteristics, including high expression and rapid growth [1,3]. Compared with intracellular expression, secretion of recombinant protein into the extracellular space provides several advantages, such as lack of proteolytic degradation and simple purification [2,[4][5][6].…”

Section: Introductionmentioning

confidence: 99%

Enhancing extracellular protein production in Escherichia coli by deleting the d‐alanyl‐d‐alanine carboxypeptidase gene dacC

Xiao

Wang

et al. 2019

Engineering in Life Sciences

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d‐Alanyl‐d‐alanine carboxypeptidase DacC is important for synthesis and stabilization of the peptidoglycan layer of Escherichia coli. In this work, dacC of E. coli BL21 (DE3) was successfully deleted, and the effects of this deletion on extracellular protein production in E. coli were investigated. The extracellular activities and fluorescence value of recombinant amylase, green fluorescent protein, and α‐galactosidase of the deletion mutants were increased by 82.3, 29.1, and 37.7%, respectively, compared with that of control cells. The outer membrane permeability and intracellular soluble peptidoglycan accumulation of deletion mutant were also enhanced compared with those of control cells, respectively. Based on fluorescence‐assisted cell sorting analyses, we found that the morphology of the E. coli deletion mutant cells was altered compared with that of control cells. Local transparent bulges in the poles of the E. coli mutant with deletion of the dacC gene were found by transmission electron microscopy analysis. These bulges in the poles could explain the improvement in the production of extracellular protein by the E. coli mutant with deletion of the dacC gene. These findings provide important insights into the extracellular production of proteins using E. coli as microbial cell factories.

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“…For instance, since the thermodynamic equilibrium of glucose to fructose isomerization increases towards fructose with increasing temperature, xylose isomerase variants with high thermal resistance are desirable. Besides searching for a thermostable natural enzyme with a reasonable activity [92,93], it is also possible to increase the thermostability of an enzyme that already has high activity [94][95][96]. In order to prevent enzyme denaturation induced by glycation (covalent linkage formation between lysine residues and the substrate glucose) as well as encouraged by the notion that the Arg/Lys ratio is higher in thermostable proteins, Mrabet et al substituted some lysines to arginines in XI from Actinoplanes missouriensis [95].…”

Section: Rational Enzyme Engineeringmentioning

confidence: 99%

“…Considering this principle, we have designed mutations to introduce positively charged residues (arginine and lysine) or to remove negatively charged ones (glutamate and aspartate). Taking the location and predicted effect on stability of the mutations into consideration, 93 PirXI variants were constructed and tested for improved activity at lower pH.…”

mentioning

confidence: 99%

Xylose isomerase from Piromyces: Characterization and engineering for improving S. cerevisiae-based lignocellulosic bioethanol production

Lee¹

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Xylose isomerases are tetrameric metalloenzymes that catalyze aldoseketose interconversion. Their activity is widely used in industrial biocatalysis, especially for the preparation of high-fructose syrups from glucose-containing starch hydrolysates. The activity with xylose is industrially relevant because it converts xylose that cannot be fermented by yeast to xylulose, which is accepted as a substrate for alcoholic fermentation. Several crystal structures of xylose isomerases have been solved and the catalytic mechanism has been investigated, opening the way to engineering more efficient variants of these enzymes. The properties of xylose isomerases and the potential of protein engineering to improve xylose metabolism by yeast are discussed here.

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Properties of a novel thermostable glucose isomerase mined from Thermus oshimai and its application to preparation of high fructose corn syrup

Cited by 52 publications

References 28 publications

Highly Selective Isomerization of Glucose into Fructose Catalyzed by a Mimic Glucose Isomerase

Highly Selective Isomerization of Glucose into Fructose Catalyzed by a Mimic Glucose Isomerase

Enhancing extracellular protein production in Escherichia coli by deleting the d‐alanyl‐d‐alanine carboxypeptidase gene dacC

Xylose isomerase from Piromyces: Characterization and engineering for improving S. cerevisiae-based lignocellulosic bioethanol production

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