Cyclization reaction catalyzed by branching enzyme

被引：86

作者：

Takata, H ^{[1
]}

Takaha, T ^{[1
]}

Okada, S ^{[1
]}

Takagi, M ^{[1
]}

Imanaka, T ^{[1
]}

机构：

[1] OSAKA UNIV,FAC ENGN,DEPT BIOTECHNOL,SUITA,OSAKA 565,JAPAN

来源：

JOURNAL OF BACTERIOLOGY | 1996年 / 178卷 / 06期

关键词：

D O I：

10.1128/jb.178.6.1600-1606.1996

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The action of branching enzyme (EC 2.4.1.18) from Bacillus stearothermophilus on amylose was analyzed. The enzyme reduced the molecular size of amylose without increasing the reducing power, This result could not be explained by the normal branching reaction model, When the product was treated,vith glucoamylase (an exo-type amylase), a resistant component remained. The glucoamylase-resistant component was easily digested by an endo-type alpha-amylase or by isoamylase plus glucoamylase. These results suggested that the glucoamylase-resistant component was a cyclic glucan composed of alpha-1,4- and alpha-1,6-glucosidic linkages. In other words, it was suggested that branching enzyme catalyzed cyclization of the alpha-1,4-glucan chain of the amylose molecule to form an alpha-1,6-glucosidic linkage, thereby forming two smaller molecules. Mass spectrometry also supported the cyclic nature of the product.

引用

页码：1600 / 1606

页数：7

共 15 条

[1]

[Anonymous], 1991, OXFORD SURVEYS PLANT

[2] MECHANISM OF AMYLOSE BRANCHING BY POTATO Q-ENZYME [J].

BOROVSKY, D ;

SMITH, EE ;

WHELAN, WJ .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 1976, 62 (02) :307-312

[3] TEMPERATURE-DEPENDENCE OF ACTION OF Q-ENZYME AND NATURE OF SUBSTRATE FOR Q-ENZYME [J].

BOROVSKY, D ;

SMITH, EE ;

WHELAN, WJ .

FEBS LETTERS, 1975, 54 (02) :201-205

[4] PURIFICATION AND PROPERTIES OF POTATO 1,4-ALPHA-D-GLUCAN - 1,4-ALPHA-D-GLUCAN 6-ALPHA-(1,4-ALPHA-GLUCANO)- TRANSFERASE - EVIDENCE AGAINST A DUAL CATALYTIC FUNCTION IN AMYLOSE-BRANCHING ENZYME [J].

BOROVSKY, D ;

SMITH, EE ;

WHELAN, WJ .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 1975, 59 (02) :615-625

[5] MECHANISM OF Q-ENZYME ACTION AND ITS INFLUENCE ON THE STRUCTURE OF AMYLOPECTIN [J].

BOROVSKY, D ;

SMITH, EE ;

WHELAN, WJ ;

FRENCH, D ;

KIKUMOTO, S .

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1979, 198 (02) :627-631

[6] THE POSSIBLE RELATIONSHIP OF STARCH AND PHYTOGLYCOGEN IN SWEET CORN .2. THE ROLE OF BRANCHING ENZYME-I [J].

BOYER, CD ;

SIMPSON, EKG ;

DAMEWOOD, PA .

STARKE, 1982, 34 (03) :81-85

[7] STARCH- AND GLYCOGEN-DEBRANCHING AND BRANCHING ENZYMES - PREDICTION OF STRUCTURAL FEATURES OF THE CATALYTIC (BETA/ALPHA)(8)-BARREL DOMAIN AND EVOLUTIONARY RELATIONSHIP TO OTHER AMYLOLYTIC ENZYMES [J].

JESPERSEN, HM ;

MACGREGOR, EA ;

HENRISSAT, B ;

SIERKS, MR ;

SVENSSON, B .

JOURNAL OF PROTEIN CHEMISTRY, 1993, 12 (06) :791-805

[8] GELATION OF AMYLOSE [J].

MILES, MJ ;

MORRIS, VJ ;

RING, SG .

CARBOHYDRATE RESEARCH, 1985, 135 (02) :257-269

[9]

Morris V. J., 1990, Trends in Food Science & Technology, V1, P2, DOI 10.1016/0924-2244(90)90002-G

[10] BACTERIAL GLYCOGEN-SYNTHESIS AND ITS REGULATION [J].

PREISS, J .

ANNUAL REVIEW OF MICROBIOLOGY, 1984, 38 :419-458

← 1 2 →