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Enzymatic hydrolysis of anchovy fine powder at high and ambient pressure, and characterization of the hydrolyzates
Author(s) -
Kim Namsoo,
Son SoHee,
Maeng JinSoo,
Cho YongJin,
Kim ChongTai
Publication year - 2016
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.7173
Subject(s) - chemistry , hydrolysis , chromatography , hydrolysate , enzymatic hydrolysis , proteases , protease , nitrogen , trichloroacetic acid , ambient pressure , enzyme , sonication , food science , organic chemistry , physics , thermodynamics
BACKGROUND At specific conditions of high pressure, the stability and activity of some enzymes are reportedly known to increase. The aim of this study was to apply pressure‐tolerant proteases to hydrolyzing anchovy fine powder ( AFP ) and to determine product characteristics of the resultant hydrolyzates. RESULTS Anchovy fine powder enzyme hydrolyzates ( AFPEHs ) were produced at 300 MPa and ambient pressure using combinations of Flavourzyme 500MG , Alcalase 2. 4L , Marugoto E and Protamex. When the same protease combination was used for hydrolysis, the contents of total soluble solids, total water‐soluble nitrogen and trichloroacetic acid‐soluble nitrogen in the AFPEHs produced at 300 MPa were conspicuously higher than those in the AFPEHs produced at ambient pressure. This result and electrophoretic characteristics indicated that the high‐pressure process of this study accelerates protein hydrolysis compared with the ambient‐pressure counterpart. Most peptides in the hydrolyzates obtained at 300 MPa had molecular masses less than 5 kDa . Functionality, sensory characteristics and the content of total free amino acids of selected hydrolyzates were also determined. CONCLUSION The high‐pressure hydrolytic process utilizing pressure‐tolerant proteases was found to be an efficient method for producing protein hydrolyzates with good product characteristics. © 2015 Society of Chemical Industry