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

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Title Purification and properties of an amylase inhibitor from colocasia (Colocasia esculenta) tubers.
 
Creator Narayana Rao, M.
Shurpalekar, K. S.
Sundaravalli, O. E.
 
Subject 05 Enzymes
23 Vegetables
 
Description 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.
 
Date 1970
 
Type Article
PeerReviewed
 
Format application/pdf
 
Language en
 
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Identifier http://ir.cftri.com/5140/1/Indian_Journal_of_Biochemistry_1970_7_241-243.pdf
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.