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Hydrolysates from Proteolysis of Heat‐denatured Whey Proteins
Author(s) -
MUTILANGI W.A.M.,
PANYAM D.,
KILARA A.
Publication year - 1995
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.1365-2621.1995.tb06302.x
Subject(s) - proteolysis , hydrolysate , chemistry , hydrolysis , whey protein , trypsin , chymotrypsin , chromatography , enzyme , enzymatic hydrolysis , whey protein isolate , polyacrylamide gel electrophoresis , hydrolyzed protein , gel electrophoresis , substrate (aquarium) , biochemistry , biology , ecology
Whey protein isolate was denatured at 85°C, pH 4.6 for 30 min to produce heat denatured whey protein isolate (HDWPI) which was hydrolyzed with trypsin, chymotrypsin, Alcalase or Neutrase to 2.8, 4.3, 6.0 or 8.0% degree of hydrolysis (DH). Analysis of freeze‐dried fractions revealed a linear increase in primary amino groups, non‐protein nitrogen and ash contents. Polyacrylamide gel electrophoresis showed that high and intermediate molecular weight peptides were converted to lower molecular weights with progress of hydrolysis. Differences in proteolysis patterns were observed with different enzymes. The time required to achieve equivalent hydrolysis at 1, 2, 3 or 4% enzyme/substrate ratio varied with the type of enzyme and DH.