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Proteolytic Enzymes from Cnidoscolus chayamansa “Chaya”
Author(s) -
CHIÑAS FCA. AIDA ITURBE,
CANALES AGUSTÍN LÓPEZMUNGUIA
Publication year - 1986
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1986.tb10885.x
Subject(s) - casein , chemistry , isoelectric point , hydrolysis , proteases , gelatin , proteolytic enzymes , biochemistry , chromatography , enzyme , ammonium sulfate precipitation , ammonium , urea , food science , size exclusion chromatography , organic chemistry
Proteolytic activity from “chaya” leaves was best extracted at pH 8 (0.05M phosphate buffer). Good storage stability was shown at pH 10 retaining 70% of initial activity after 30 days. Proteolytic enzymes were partially purified by isoelectric and ammonium sulfate precipitation. Optimal proteolytic activity was found at pH 7.5. Proteases were tested for their ability to hydrolyze several food proteins. At pH 7.5 the hydrolysis of urea‐denatured hemoglobin was extensive; casein and soybean proteins were hydrolyzed to a moderate degree and bovine serum albumin, gelatin and fish protein isolate to a lesser degree rate.