Amino acid composition and functional properties of giant red sea cucumber (Parastichopus californicus) collagen hydrolysates |
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Authors: | Zunying Liu Yicheng Su Mingyong Zeng |
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Institution: | 1. College of Food Science and Engineering, Ocean University of China, Qingdao,266003, P. R. China 2. Seafood Research and Education Center, Oregon State University,2001 Marine Drive, Room 253, Astoria, OR,97103, U.S.A. |
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Abstract: | Giant red sea cucumber (Parastichopus californicus) is an under-utilized species due to its high tendency to autolysis. The aim of this study was to evaluate the functional
properties of collagen hydrolysates from this species. The degree of hydrolysis (DH), amino acid composition, SDS-PAGE, emulsion
activity index (EAI), emulsion stability index (ESI), foam expansion (FE), and foam stability (FS) of hydrolysates were investigated.
The effects of pH on the EAI, ESI FE and FS of hydrolysates were also investigated. The results indicated that the β and α
1 chains of the collagen were effectively hydrolyzed by trypsin at 50°c with an Enzyme/Substrate (E/S) ration of 1:20 (w:w).
The DH of collagen was up to 17.3% after 3 h hydrolysis with trypsin. The hydrolysates had a molecular weight distribution
of 1.1–17 kDa, and were abundant in glycine (Gly), proline (Pro), glutamic acid (Glu), alanine (Ala) and hydroxyproline (Hyp)
residues. The hydrolysates were fractionated into three fractions (< 3 kDa, 3–10 kDa, and > 10 kDa), and the fraction of 3–10
kDa exhibited a higher EAI value than the fraction of > 10 kDa (P<0.05). The fraction of > 10 kDa had higher FE and FS values than other fractions (P<0.05). The pH had an important effect on the EAI, ESI, FE and FS. All the fractions showed undesirable emulsion and forming
properties at pH 4.0. Under pH 7.0 and pH 10.0, the 3–10 kDa fraction showed higher EAI value and the fraction of > 10 kDa
showed higher FE value, respectively. They are hoped to be utilized as functional ingredients in food and nutraceutical industries. |
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Keywords: | giant red sea cucumber collagen hydrolysates functional properties |
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