Effect of electron irradiation on the gel properties of Collichthys lucidus surimi

被引：7

作者：

Deng, Siyao ^{[1
,2
,3
]}

Lv, Liangyu ^{[1
,3
]}

Yang, Wenge ^{[1
,2
,3
]}

Xu, Dalun ^{[1
]}

Lou, Qiaoming ^{[1
]}

Zhang, Jinjie ^{[1
]}

机构：

[1] Ningbo Univ, Sch Marine Sci, Ningbo 315211, Zhejiang, Peoples R China

[2] Ningbo Univ, Collaborat Innovat Ctr Zhejiang Marine High Effic, Ningbo 315211, Zhejiang, Peoples R China

[3] Ningbo Univ, Key Lab Anim Prot Food Deep Proc Technol Zhejiang, Ningbo 315211, Zhejiang, Peoples R China

来源：

RADIATION PHYSICS AND CHEMISTRY | 2017年 / 130卷

基金：

中国国家自然科学基金;

关键词：

Electron irradiation; Surimi gel; Gel properties; Protein secondary structure; RAMAN-SPECTROSCOPY; STRUCTURAL-CHANGES; PHYSICOCHEMICAL PROPERTIES; MUSCLE PROTEINS; FORMING ABILITY; GELATION; STORAGE; HEAT;

D O I：

10.1016/j.radphyschem.2016.08.022

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

This study evaluated the effect of electron irradiation on the gel properties of Collichthys lucidus surimi. The results showed that irradiation decreased the trichloroacetic acid-soluble peptide content of the surimi gel. At 5 kGy, a more compact and ordered gel network structure was achieved, resulting in a higher gel strength, whiteness, and water-holding capacity than non-irradiated surimi gel. During heat induced formation of the gel, the alpha-helix content decreased, whilst the beta-sheet and beta-turn content increased. Irradiation treatments also decreased the alpha-helix content and increased beta-sheet content, and this transformation is beneficial for the protein denaturation and gel formation. Collectively, the results suggest that electron irradiation, at an optimal dose of 5 kGy, could be an effective method for application in the surimi manufacturing industry (C) 2016 Elsevier Ltd. All rights reserved.

引用

页码：316 / 320

页数：5

共 20 条

[1] FAST DETERMINATION OF THE QUANTITATIVE SECONDARY STRUCTURE OF PROTEINS BY USING SOME PARAMETERS OF THE RAMAN AMIDE I-BAND
ALIX, AJP
PEDANOU, G
BERJOT, M
[J]. JOURNAL OF MOLECULAR STRUCTURE, 1988, 174 : 159 - 164
[2] Thermal gel degradation (modori) in sardine surimi gels
Alvarez, C
Couso, I
Tejada, M
[J]. JOURNAL OF FOOD SCIENCE, 1999, 64 (04) : 633 - 637
[3] Effect of some protein additives on proteolysis and gel-forming ability of lizardfish (Saurida tumbil)
Benjakul, S
Visessanguan, W
Tueksuban, J
Tanaka, M
[J]. FOOD HYDROCOLLOIDS, 2004, 18 (03) : 395 - 401
[4] In situ investigation of protein structure in Pacific whiting surimi and gels using Raman spectroscopy
Bouraoui, M
Nakai, S
LiChan, E
[J]. FOOD RESEARCH INTERNATIONAL, 1997, 30 (01) : 65 - 72
[5] Structural properties of aggregates from frozen stored hake muscle proteins
Careche, M
García, ML
Herrero, A
Solas, MT
Carmona, P
[J]. JOURNAL OF FOOD SCIENCE, 2002, 67 (08) : 2827 - 2832
[6] Physicochemical properties and gel-forming ability of surimi from three species of mackerel caught in Southern Thailand
Chaijan, Manat
Panpipat, Worawan
Benjakul, Soottawat
[J]. FOOD CHEMISTRY, 2010, 121 (01) : 85 - 92
[7] Raman spectroscopic study of structural changes in hake (Merluccius merluccius L.) muscle proteins during frozen storage
Herrero, AM
Carmona, P
Careche, M
[J]. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2004, 52 (08) : 2147 - 2153
[8] Physicochemical changes in Alaska pollock surimi and surimi gel as affected by electron beam
Jaczynski, J
Park, JW
[J]. JOURNAL OF FOOD SCIENCE, 2004, 69 (01) : C53 - C57
[9] Physicochemical properties of surimi seafood as affected by electron beam and heat
Jaczynski, J
Park, JW
[J]. JOURNAL OF FOOD SCIENCE, 2003, 68 (05) : 1626 - 1630
[10] VIBRATIONAL SPECTROSCOPY AND CONFORMATION OF PEPTIDES, POLYPEPTIDES, AND PROTEINS
KRIMM, S
BANDEKAR, J
[J]. ADVANCES IN PROTEIN CHEMISTRY, 1986, 38 : 181 - 364

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