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Isolation and Heat Stability of Trypsin Inhibitors in Amaranth (Amaranthus hypochondriacus)
Author(s) -
KOEPPE SUSAN J.,
RUPNOW JOHN H.,
WALKER C. E.,
DAVIS ART
Publication year - 1985
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.1365-2621.1985.tb10523.x
Subject(s) - amaranthus hypochondriacus , amaranth , trypsin , chromatography , chemistry , amaranthaceae , trypsin inhibitor , affinity chromatography , chymotrypsin , kunitz sti protease inhibitor , polyacrylamide gel electrophoresis , biochemistry , enzyme , biology , botany
Trypsin inhibitors were isolated from seeds of Amaranthus hypochondriacus by extraction at pH 7.5, heat treatment at 70°C for 15 min and affinity chromatography with trypsin‐Sepharose 4B. Inhibitors of trypsin and chymotrypsin were identified in polyacrylamide gels following electrophoresis using a stain procedure that employed the chromogenic substrate acetyl‐D, L‐phenylalanine‐2‐napthyl ester. Three of the thirteen trypsin inhibitors identified in the electrophoresis gels, also had antichymotryptic activity. The inhibitor preparation was very thermostable retaining 20% of its original activity after 7 hr at 100°C.