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J Agric Food Chem. 2002 Aug 14;50(17):4906-8.

Isolation, purification, and biochemical characterization of a novel water soluble protein from Inca peanut (Plukenetia volubilis L.).

Author information

1
Department of Nutrition, Food and Exercise Sciences, College of Human Sciences, Florida State University, Tallahassee, Florida 32306-1493, USA. ssathe@mailer.fsu.edu

Abstract

A water soluble storage albumin from Inca peanut (IPA) accounted for approximately 25% (w/w) of defatted seed flour weight, representing 31% of the total seed protein. IPA is a 3S storage protein composed of two glycosylated polypeptides, with estimated molecular weights (MW) of 32800 and 34800 Da, respectively. IPA has an estimated sugar content of 4.8% +/- 0.92% (n = 6). IPA is a basic protein (pI of approximately 9.4) and contains all of the essential amino acids in adequate amounts when compared to the FAO/WHO recommended pattern for a human adult. The tryptophan content of IPA is unusually high (44 mg/g of protein), whereas the phenylalanine content is low (9 mg/g of protein). IPA is a highly digestible protein in vitro.

PMID:
12166980
[Indexed for MEDLINE]

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