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원양산 오징어(Illex argentinus) 간췌장 유래 Exopeptidase 분획물의 쓴맛개선 효과Debittering of Enzymatic Hydrolysate Using Exopeptidase Active Fractions from the Argentina Shortfin Squid Illex argentinus Hepatopancreas

Other Titles
Debittering of Enzymatic Hydrolysate Using Exopeptidase Active Fractions from the Argentina Shortfin Squid Illex argentinus Hepatopancreas
Authors
김진수허민수김민지김기현강상인박성환이현지
Issue Date
2014
Publisher
한국수산과학회
Keywords
Argentina shortfin squid; Hepatopancreas; Exopeptidase; Bitterness hydrolysate; Debittering
Citation
한국수산과학회지, v.47, no.2, pp 135 - 143
Pages
9
Indexed
KCI
Journal Title
한국수산과학회지
Volume
47
Number
2
Start Page
135
End Page
143
URI
https://scholarworks.gnu.ac.kr/handle/sw.gnu/19929
DOI
10.5657/KFAS.2014.0134
ISSN
0374-8111
Abstract
Exopeptidase active fractions from the hepatopancreas of the Argentina shortfin squid Illex argentinus , were obtained with acetone (AC 30-40%), ammonium sulfate (AS 60-70% saturation), anion exchange chromatography (AE-II, 0.2 M NaCl) and gel filtration chromatography (GF-I, 30-50 kDa) fractionation methods. A bitter peptide solution that has a bitterness equivalent to that of 2% glycylphenylalanine and prepared by tryptic hydrolysis of milk casein, was treated with the exopeptidase active fractions. The GF -I fraction was the best based on aminopeptidase activity (35.3 U/mg), percentage of recovery (30.7%) and a sensory evaluation (1.7). The amount of released amino acids increased as incubation time increased, and the bitterness of the enzyme reaction mixtures decreased. Incubation with the GF-I fraction for 24 h resulted in the hydrolysis of several peptides as revealed by the reverse-phase high perfor- mance liguid chromatography profile, with three peaks (3, 5 and 6) decreasing in area (%) and three peaks (1, 2 and 4) increasing in area (%). Therefore, the GF-I fraction appeared to be ideally suited to reduce bitterness in protein hydrolysates by catalyzing the hydrolysis of bitter peptides.
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자연과학대학 (식품영양학과)
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