Properties of maltose phosphorylase from Propionibacterium freudenreichii

被引：15

作者：

Aisaka, K

Masuda, T

Chikamune, T

机构：

[1] Tokyo Research Laboratories, Kyowa Hakko Kogyo Co. Ltd., Machida-shi, Tokyo 194

来源：

JOURNAL OF FERMENTATION AND BIOENGINEERING | 1996年 / 82卷 / 02期

关键词：

maltose phosphorylase; Propionibacterium freudenreichii; disaccharide;

D O I：

10.1016/0922-338X(96)85043-4

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Maltose phosphorylase (EC 2.4.1.8) from Propionibacterium freudenreichii was purified and characterized. The enzyme catalyzed both the phosphorolysis and the synthesis of maltose. In particular, in the synthetic reaction, the enzyme could use any of nine sugars other than D-glucose as a sugar acceptor, which resulted in the formation of new disaccharides, in which the first carbon of D-glucose and the fourth carbon of the other sugar were connected by an a-glycosidic linkage.

引用

页码：171 / 173

页数：3

共 8 条

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[2]

DOUDOROFF M, 1961, ENZYMES, P229

[3]

FITTING C, 1952, J BIOL CHEM, V199, P153

[4] PURIFICATION AND PROPERTIES OF MALTOSE PHOSPHORYLASE FROM LACTOBACILLUS-BREVIS [J].