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Purification and properties of an amylase inhibitor from colocasia (Colocasia esculenta) tubers.

Narayana Rao, M. and Shurpalekar, K. S. and Sundaravalli, O. E. (1970) Purification and properties of an amylase inhibitor from colocasia (Colocasia esculenta) tubers. Indian Journal of Biochemistry, 7. pp. 241-243.

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Abstract

A method for the isolation and purification of an amylase inhibitor from colocasia (Colocasia esculenta) tubers is described. The purified amylase inhibitor is a white, amorphous and hygroscopic powder containing 15.6% nitrogen. It is deficient in methionine and gives a typical protein spectrum with a maximum at 280 mg and minimum at 252 mg. The inhibitor which is electrophoretically homogeneous over a wide range of pH is stable to boiling temperatures and specifically inhibits salivary amylase. The nature of inhibition appears to be of mixed type. The activity of the inhibitor is destroyed by proteolytic enzymes, ficin and pepsin.

Item Type: Article
Uncontrolled Keywords: colocasia, amylase inhibitor,
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 05 Enzymes
600 Technology > 08 Food technology > 23 Vegetables
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 22 May 2012 09:32
Last Modified: 22 May 2012 09:32
URI: http://ir.cftri.com/id/eprint/5140

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