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微生物 α-淀粉酶的分子改良提高稳定性和催化效率。

Molecular improvements in microbial α-amylases for enhanced stability and catalytic efficiency.

机构信息

Centre for Biofuels, National Institute for Interdisciplinary Science and Technology, CSIR, Trivandrum 695 019, India.

Centre for Biofuels, National Institute for Interdisciplinary Science and Technology, CSIR, Trivandrum 695 019, India.

出版信息

Bioresour Technol. 2017 Dec;245(Pt B):1740-1748. doi: 10.1016/j.biortech.2017.04.098. Epub 2017 Apr 27.


DOI:10.1016/j.biortech.2017.04.098
PMID:28478894
Abstract

α-Amylases is one of the most important industrial enzyme which contributes to 25% of the industrial enzyme market. Though it is produced by plant, animals and microbial source, those from microbial source seems to have potential applications due to their stability and economic viability. However a large number of α-amylases from different sources have been detailed in the literature, only few numbers of them could withstand the harsh industrial conditions. Thermo-stability, pH tolerance, calcium independency and oxidant stability and starch hydrolyzing efficiency are the crucial qualities for α-amylase in starch based industries. Microbes can be genetically modified and fine tuning can be done for the production of enzymes with desired characteristics for specific applications. This review focuses on the native and recombinant α-amylases from microorganisms, their heterologous production and the recent molecular strategies which help to improve the properties of this industrial enzyme.

摘要

α-淀粉酶是最重要的工业酶之一,占工业酶市场的 25%。尽管它是由植物、动物和微生物来源产生的,但由于其稳定性和经济可行性,那些来自微生物来源的酶似乎具有潜在的应用前景。然而,文献中已经详细描述了大量来自不同来源的α-淀粉酶,只有少数几种能够承受恶劣的工业条件。热稳定性、pH 耐受性、钙离子独立性和氧化稳定性以及淀粉水解效率是淀粉基工业中α-淀粉酶的关键特性。微生物可以进行基因改造,并且可以对酶进行微调,以生产出具有特定应用所需特性的酶。本文综述了微生物来源的天然和重组α-淀粉酶、它们的异源生产以及最近有助于改善这种工业酶特性的分子策略。

相似文献

[1]
Molecular improvements in microbial α-amylases for enhanced stability and catalytic efficiency.

Bioresour Technol. 2017-4-27

[2]
Application of microbial α-amylase in industry - A review.

Braz J Microbiol. 2010-12-1

[3]
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[4]
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[6]
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[7]
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[8]
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[9]
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[10]
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引用本文的文献

[1]
Enhanced saccharification levels of corn starch using as a strategy a novel amylolytic complex (AmyHb) from the thermophilic fungus var. in association with commercial enzyme.

3 Biotech. 2024-9

[2]
Biochemical Characterization of a Novel Thermostable 1,4-α-Glucoamylase from Aspergillus brasiliensis Strain Isolated in the Brazilian Atlantic Forest.

Appl Biochem Biotechnol. 2024-10

[3]
as a Platform for Heterologous Expression of Enzymes Used for Industry.

Microorganisms. 2024-2-7

[4]
Development of the thermophilic fungus Myceliophthora thermophila into glucoamylase hyperproduction system via the metabolic engineering using improved AsCas12a variants.

Microb Cell Fact. 2023-8-11

[5]
Isolation of novel cold-tolerance genes from rhizosphere microorganisms of Antarctic plants by functional metagenomics.

Front Microbiol. 2022-11-18

[6]
A Review on Psychrophilic β-D-Galactosidases and Their Potential Applications.

Appl Biochem Biotechnol. 2023-4

[7]
Characterization of an Amylolytic Enzyme from Massilia timonae of the GH13_19 Subfamily with Mixed Maltogenic and CGTase Activity.

Appl Biochem Biotechnol. 2023-3

[8]
Study on Active Particles in Air Plasma and Their Effect on α-Amylase.

Foods. 2022-9-18

[9]
Hunt for α-amylase from metagenome and strategies to improve its thermostability: a systematic review.

World J Microbiol Biotechnol. 2022-8-24

[10]
Invitro bioprocessing of corn as poultry feed additive by the influence of carbohydrate hydrolyzing metagenome derived enzyme cocktail.

Sci Rep. 2022-1-10

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