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Purification and characteristics of an endogenous alpha-amylase and trypsin inhibitor from wheat seeds

✍ Scribed by Warchalewski, J. R.

Publisher: John Wiley and Sons
Year: 1987
Tongue: English
Weight: 865 KB
Volume: 31
Category: Article
ISSN: 0027-769X
DOI: 10.1002/food.19870311017

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✦ Synopsis

Purification and characteristics of an endogenous alpha-amylase and trypsin inhibitor from wheat seeds'*2 J. R. WARCHALEWSKI

The bifunctional endogenous alpha-amylase and trypsin inhibitor was purified 151-fold from a crude extract of wheat grain by (NH,),SO, fractionation, ion exchange chromatography and gel filtration. The inhibitor coded A/T-WI was an albumin protein, relatively heat stable with a molar mass of 23233 g/mol and optimum activity towards native alpha-amylase and trypsin at pH 5.1 and 7.1,respectively. Amino acid analysis indicated the presence of about 15 half-cystine residues per mole. The protein was homogeneous as assessed by polyacrylamide gel electrophoresis. In the presence of detergent the inhibitor was dissociated into two subunits. A "double head" in nature the inhibitor was almost inactive in the presence of detergent with reducing agent. At neutral pH over 80 % of inhibitor was adhered to wheat starch granules.

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