Exploring and exploiting starch-modifying amylomaltases from thermophiles

被引：62

作者：

Kaper, T

van der Maarel, MJEC

Euverink, GJW

Dijkhuizen, L

机构：

[1] TNO, Nutr & Food Res, Innovat Ingredients & Prod Dept, NL-9723 CC Groningen, Netherlands

[2] RUG, TNO, Ctr Carbohydrate Bioengn, NL-9750 AA Haren, Netherlands

[3] Univ Groningen, Groningen Biomol Sci & Biotechnol Inst, Microbial Physiol Res Grp, NL-9751 NN Haren, Netherlands

来源：

BIOCHEMICAL SOCIETY TRANSACTIONS | 2004年 / 32卷

关键词：

amylomaltase; enzyme; gel; 4-alpha gluwcanotranslerase; glycosidic linkage; starch;

D O I：

10.1042/BST0320279

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：

Starch is a staple food present in water-insoluble granules in many economically important crops. It is composed of two glucose polymers: the linear alpha-1,4-linked amylose and amylopectin with a backbone of alpha-1,4-glycosidic bonds and alpha-1,6-linked side chains. To dissolve starch completely in water it needs to be heated; when it cools down too much the starch solution forms a thermo-irreversible gel. Amylomaltases (EC 2.4.1.25) are enzymes that transfer a segment of an alpha-1,4-D-glucan to a new 4-position in an acceptor, which may be glucose or another alpha-1,4-D-glucan. Acting upon starch, amylomaltases can produce cycloamylose or a thermoreversible starch gel, both of which are of commercial interest.

引用

收藏

页码：279 / 282

页数：4

相关论文

共 31 条

[1] A cycloamylose-forming hyperthermostable 4-α-glucanotransferase of Aquifex aeolicus expressed in Escherichia coli [J].

Bhuiyan, SH ;

Kitaoka, M ;

Hayashi, K .

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 2003, 22 (1-2) :45-53

[2] Maltose/maltodextrin system of Escherichia coli:: Transport, metabolism, and regulation [J].

Boos, W ;

Shuman, H .

MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS, 1998, 62 (01) :204-+

[3] Biochemical characterization of the Chlamydomonas reinhardtii α-1,4 glucanotransferase supports a direct function in amylopectin biosynthesis [J].

Colleoni, C ;

Dauvillée, D ;

Mouille, G ;

Morell, M ;

Samuel, M ;

Slomiany, MC ;

Liénard, L ;

Wattebled, F ;

d'Hulst, C ;

Ball, S .

PLANT PHYSIOLOGY, 1999, 120 (04) :1005-1013

[4]

Crabb WD, 1997, TRENDS BIOTECHNOL, V15, P349, DOI 10.1016/S0167-7799(97)01082-2

[5] A critical role for disproportionating enzyme in starch breakdown is revealed by a knock-out mutation in Arabidopsis [J].

Critchley, JH ;

Zeeman, SC ;

Takaha, T ;

Smith, AM ;

Smith, SM .

PLANT JOURNAL, 2001, 26 (01) :89-100

[6] STRUCTURES AND MECHANISMS OF GLYCOSYL HYDROLASES [J].

DAVIES, G ;

HENRISSAT, B .

STRUCTURE, 1995, 3 (09) :853-859

[7]

Euverink G. J. W., 1998, Use of modified starch as an agent for forming a thermoreversible gel, Patent No. [WO9815347, 9815347]

[8] V-amylose at atomic resolution:: X-ray structure of a cycloamylose with 26 glucose residues (cyclomaltohexaicosaose) [J].

Gessler, K ;

Usón, I ;

Takaha, T ;

Krauss, N ;

Smith, SM ;

Okada, S ;

Sheldrick, GM ;

Saenger, W .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (08) :4246-4251

[9] Updating the sequence-based classification of glycosyl hydrolases [J].

Henrissat, B ;

Bairoch, A .

BIOCHEMICAL JOURNAL, 1996, 316 :695-696

[10] 4-alpha-glucanotransferase from the hyperthermophilic archaeon Thermococcus litoralis - Enzyme purification and characterization, and gene cloning, sequencing and expression in Escherichia coli [J].

Jeon, BS ;

Taguchi, H ;

Sakai, H ;

Ohshima, T ;

Wakagi, T ;

Matsuzawa, H .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 1997, 248 (01) :171-178

← 1 2 3 4 →