Improvement of microbial α-amylase stability: Strategic approaches

被引：38

作者：

Dey, Tapati Bhanja ^{[1
]}

Kumar, Arvind ^{[1
]}

Banerjee, Rintu ^{[2
]}

Chandna, Piyush ^{[1
]}

Kuhad, Ramesh Chander ^{[1
,3
]}

机构：

[1] Univ Delhi, Dept Microbiol, Lignocellulose Biotechnol Lab, South Campus,Benito Juarez Rd, New Delhi 110021, India

[2] Indian Inst Technol, Agr & Food Engn Dept, Microbial Biotechnol & Downstream Proc Lab, Kharagpur 721302, W Bengal, India

[3] Cent Univ Haryana, Pali 123029, Haryana, India

来源：

PROCESS BIOCHEMISTRY | 2016年 / 51卷 / 10期

关键词：

alpha-Amylase; Industrial biotechnology; Stability; Thermostable; Starch; Protein engineering; Directed evolution; BACILLUS-LICHENIFORMIS; THERMAL-STABILITY; DIRECTED EVOLUTION; CHEMICAL-MODIFICATION; HYPERTHERMOSTABLE MUTANTS; STEAROTHERMOPHILUS US100; ENHANCED STABILITY; CATALYTIC-ACTIVITY; LYSINE RESIDUES; SPORE SURFACE;

D O I：

10.1016/j.procbio.2016.06.021

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Microbial alpha-amylase being a vital enzyme in industrial biotechnology, has also received enormous attention in academic field. Although a huge number of alpha-amylases from different sources have been mentioned in the literature, only few of them are able to meet the industrial demands. Thermostability, pH tolerance, calcium independency and oxidant stability and very high starch hydrolyzing efficiency are the important criteria for the diverse applications of alpha-amylase in starch based industries. Owing to biotechnological importance, its stability is a major concern for its economic viability. Stable microbial alpha-amylase can be obtained: (i) from extremophiles and genetically manipulated non extremopliles, and (ii) through improving stability by immobilization, chemical modification, protein engineering and augmenting with different additives. The present review is an attempt to compile the different strategies employed till date to obtain stable alpha-amylase. (C) 2016 Published by Elsevier Ltd.

引用

页码：1380 / 1390

页数：11

共 135 条

[1]

Aiyer PV, 2005, AFR J BIOTECHNOL, V4, P1525

[2] Production and immobilization of a novel thermoalkalophilic extracellular amylase from bacilli isolate [J].

Akkaya, Birnur ;

Yenidunya, Ali Fazil ;

Akkaya, Recep .

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 2012, 50 (04) :991-995

[3] Characteristics of a novel, highly acid- and thermo-stable amylase from thermophilic Bacillus strain HUTBS62 under different environmental conditions [J].

Al-Quadan, Farouk ;

Akel, Hazem ;

Natshi, Rasha .

ANNALS OF MICROBIOLOGY, 2011, 61 (04) :887-892

[4] Purification and Characterization of a Polyextremophilic α-Amylase from an Obligate Halophilic Aspergillus penicillioides Isolate and Its Potential for Souse with Detergents [J].

Ali, Imran ;

Akbar, Ali ;

Anwar, Mohammad ;

Prasongsuk, Sehanat ;

Lotrakul, Pongtharin ;

Punnapayak, Hunsa .

BIOMED RESEARCH INTERNATIONAL, 2015, 2015

[5] Activity of diastase α-amylase immobilized on polyanilines (PANIs) [J].

Ashly, P. C. ;

Joseph, M. J. ;

Mohanan, P. V. .

FOOD CHEMISTRY, 2011, 127 (04) :1808-1813

[6] A novel thermostable, acidophilic α-amylase from a new thermophilic "Bacillus sp Ferdowsicous" isolated from Ferdows hot mineral spring in Iran: Purification and biochemical characterization [J].

Asoodeh, Ahmad ;

Chamani, JamshidKhan ;

Lagzian, Milad .

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 2010, 46 (03) :289-297

[7] Thermostability enhancement and change in starch hydrolysis profile of the maltohexaose-forming amylase of Bacillus stearothermophilus US100 strain [J].

Ben Ali, M ;

Khemakhem, B ;

Robert, X ;

Haser, R ;

Bejar, S .

BIOCHEMICAL JOURNAL, 2006, 394 (51-56) :51-56

[8] Purification and sequence analysis of the atypical maltohexaose-forming α-amylase of the B-stearothermophilus US100 [J].

Ben Ali, M ;

Mhiri, S ;

Mezghani, M ;

Bejar, S .

ENZYME AND MICROBIAL TECHNOLOGY, 2001, 28 (06) :537-542

[9] Toward the smallest active subdomain of a TIM-barrel fold: Insights from a truncated α-amylase [J].

Ben Ali, Mamdouh ;

Ghram, Mehdi ;

Hmani, Houda ;

Khemakhem, Bassem ;

Haser, Richard ;

Bejar, Samir .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2011, 411 (02) :265-270

[10] Directed evolution of a bacterial α-araylase:: Toward enhanced pH-performance and higher specific activity [J].

Bessler, C ;

Schmitt, J ;

Maurer, KH ;

Schmid, RD .

PROTEIN SCIENCE, 2003, 12 (10) :2141-2149

← 1 2 3 4 5 6 7 8 9 10 →