α-Amylase: An Ideal Representative of Thermostable Enzymes

被引：122
作者：
Prakash, Om [1 ]
Jaiswal, Nivedita [1 ]
机构：
[1] Banaras Hindu Univ, Dept Biochem, Fac Sci, Varanasi 221005, UP, India
来源：
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY | 2010年 / 160卷 / 08期
关键词：
alpha-Amylase; Thermostability; Structural flexibility; Rigidity; Unfolding state; ARCHAEON PYROCOCCUS-FURIOSUS; AMINO-ACID-COMPOSITION; BACILLUS-LICHENIFORMIS; CRYSTAL-STRUCTURE; PROTEIN THERMOSTABILITY; THERMAL-STABILITY; CITRATE SYNTHASE; ALTEROMONAS-HALOPLANCTIS; LACTATE-DEHYDROGENASE; ENGINEERING PROTEINS;
D O I：
10.1007/s12010-009-8735-4
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：
The conditions prevailing in the industrial applications in which enzymes are used are rather extreme, especially with respect to temperature and pH. Therefore, there is a continuing demand to improve the stability of enzymes and to meet the requirements set by specific applications. In this respect, thermostable enzymes have been proposed to be industrially relevant. In this review, alpha-amylase, a well-established representative of thermostable enzymes, providing an attractive model for the investigation of the structural basis of thermostability of proteins, has been discussed.
引用
收藏
页码：2401 / 2414
页数：14
相关论文
共 131 条
[1]   Crystal structures of the psychrophilic α-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor [J].
Aghajari, N ;
Feller, G ;
Gerday, C ;
Haser, R .
PROTEIN SCIENCE, 1998, 7 (03) :564-572
[2]   Studies on a thermostable α-amylase from the thermophilic fungus Scytalidium thermophilum [J].
Aquino, ACMM ;
Jorge, JA ;
Terenzi, HF ;
Polizeli, MLTM .
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 2003, 61 (04) :323-328
[3]   ENGINEERING PROTEINS FOR NONNATURAL ENVIRONMENTS [J].
ARNOLD, FH .
FASEB JOURNAL, 1993, 7 (09) :744-749
[4]   STRUCTURE OF CHICKEN MUSCLE TRIOSE PHOSPHATE ISOMERASE DETERMINED CRYSTALLOGRAPHICALLY AT 2.5A RESOLUTION USING AMINO-ACID SEQUENCE DATA [J].
BANNER, DW ;
BLOOMER, AC ;
PETSKO, GA ;
PHILLIPS, DC ;
POGSON, CI ;
WILSON, IA ;
CORRAN, PH ;
FURTH, AJ ;
MILMAN, JD ;
OFFORD, RE ;
PRIDDLE, JD ;
WALEY, SG .
NATURE, 1975, 255 (5510) :609-614
[5]   A complete sequence of the T tengcongensis genome [J].
Bao, QY ;
Tian, YQ ;
Li, W ;
Xu, ZY ;
Xuan, ZY ;
Hu, SN ;
Dong, W ;
Yang, J ;
Chen, YJ ;
Xue, YF ;
Xu, Y ;
Lai, XQ ;
Huang, L ;
Dong, XZ ;
Ma, YH ;
Ling, LJ ;
Tan, HR ;
Chen, RS ;
Wang, J ;
Yu, J ;
Yang, HM .
GENOME RESEARCH, 2002, 12 (05) :689-700
[6]  
BARNETT CC, 1998, Patent No. 5524532
[7]   Comparing the thermodynamic stabilities of a related thermophilic and mesophilic enzyme [J].
Beadle, BM ;
Baase, WA ;
Wilson, DB ;
Gilkes, NR ;
Shoichet, BK .
BIOCHEMISTRY, 1999, 38 (08) :2570-2576
[8]   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
[9]   CALCIUM-BINDING IN ALPHA-AMYLASES - AN X-RAY-DIFFRACTION STUDY AT 2.1-A RESOLUTION OF 2 ENZYMES FROM ASPERGILLUS [J].
BOEL, E ;
BRADY, L ;
BRZOZOWSKI, AM ;
DEREWENDA, Z ;
DODSON, GG ;
JENSEN, VJ ;
PETERSEN, SB ;
SWIFT, H ;
THIM, L ;
WOLDIKE, HF .
BIOCHEMISTRY, 1990, 29 (26) :6244-6249
[10]   Enhanced thermal stability of Clostridium beijerinckii alcohol dehydrogenase after strategic substitution of amino acid residues with prolines from the homologous thermophilic Thermoanaerobacter brockii alcohol dehydrogenase [J].
Bogin, O ;
Peretz, M ;
Hacham, Y ;
Korkhin, Y ;
Frolow, F ;
Kalb, AJ ;
Burstein, Y .
PROTEIN SCIENCE, 1998, 7 (05) :1156-1163
12345678910