DETERMINATION OF SPECIFIC ACTIVITIES OF MALT ALPHA-AMYLASES

被引：22

作者：

MACGREGOR, AW

MORGAN, JE

机构：

[1] Canadian Grain Commission, Grain Research Laboratory, Winnipeg, Manitoba, R3C 3G8

来源：

JOURNAL OF CEREAL SCIENCE | 1992年 / 16卷 / 03期

关键词：

D O I：

10.1016/S0733-5210(09)80089-1

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Highly purified samples of α-amylases 1 and 2 were prepared from malted barley using ion exchange chromatography on carboxymethyl cellulose and affinity chromatography on cyclohepta-amylose epoxy Sepharose 6B. Specific activities of the two enzymes on amylose were determined by using end-group analysis of the products formed. Per unit of protein, the specific activity of α-amylase 2 was 2·3 times higher than that of α-amylase 1. © 1992, Academic Press Limited. All rights reserved.

引用

页码：267 / 277

页数：11

共 37 条

[1]

ASP EH, 1990, CEREAL FOODS WORLD, P941

[2]

BANKS W, 1959, MAKROMOLEKUL CHEM, V31, P197

[3]

BETTNER RE, 1962, P AM SOC BREWING CHE, P5

[4]

Briggs D.E, 1961, J I BREW JIB, V67, P427

[5]

Greenwood C T, 1968, Adv Carbohydr Chem Biochem, V23, P281

[6]

Greenwood CT, 1965, J I BREWING, V71, P405, DOI [10.1002/j.2050-0416.1965.tb06366.x, DOI 10.1002/J.2050-0416.1965.TB06366.X]

[7] MULTIPLE FORMS OF ALPHA-AMYLASE IN MALTING BARLEY VAR EMMA [J].

HAYES, B ;

HARMEY, MA ;

BYRNE, H .

JOURNAL OF THE INSTITUTE OF BREWING, 1988, 94 (04) :253-259

[8] FINE-STRUCTURE OF WHEAT AMYLOPECTIN - THE MODE OF A-CHAIN TO B-CHAIN BINDING [J].

HIZUKURI, S ;

MAEHARA, Y .

CARBOHYDRATE RESEARCH, 1990, 206 (01) :145-159

[9]

Ho T. H. D., 1991, JIAS, Journal of the Iowa Academy of Science, V98, P72

[10]

JACOBSEN JV, 1982, 11TH P INT C PLANT G, P111

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