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

被引:9
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
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
收藏
页码:316 / 320
页数:5
相关论文
共 20 条
[1]   FAST DETERMINATION OF THE QUANTITATIVE SECONDARY STRUCTURE OF PROTEINS BY USING SOME PARAMETERS OF THE RAMAN AMIDE I-BAND [J].
ALIX, AJP ;
PEDANOU, G ;
BERJOT, M .
JOURNAL OF MOLECULAR STRUCTURE, 1988, 174 :159-164
[2]   Thermal gel degradation (modori) in sardine surimi gels [J].
Alvarez, C ;
Couso, I ;
Tejada, M .
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) [J].
Benjakul, S ;
Visessanguan, W ;
Tueksuban, J ;
Tanaka, M .
FOOD HYDROCOLLOIDS, 2004, 18 (03) :395-401
[4]   In situ investigation of protein structure in Pacific whiting surimi and gels using Raman spectroscopy [J].
Bouraoui, M ;
Nakai, S ;
LiChan, E .
FOOD RESEARCH INTERNATIONAL, 1997, 30 (01) :65-72
[5]   Structural properties of aggregates from frozen stored hake muscle proteins [J].
Careche, M ;
García, ML ;
Herrero, A ;
Solas, MT ;
Carmona, P .
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 [J].
Chaijan, Manat ;
Panpipat, Worawan ;
Benjakul, Soottawat .
FOOD CHEMISTRY, 2010, 121 (01) :85-92
[7]   Raman spectroscopic study of structural changes in hake (Merluccius merluccius L.) muscle proteins during frozen storage [J].
Herrero, AM ;
Carmona, P ;
Careche, M .
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 [J].
Jaczynski, J ;
Park, JW .
JOURNAL OF FOOD SCIENCE, 2004, 69 (01) :C53-C57
[9]   Physicochemical properties of surimi seafood as affected by electron beam and heat [J].
Jaczynski, J ;
Park, JW .
JOURNAL OF FOOD SCIENCE, 2003, 68 (05) :1626-1630
[10]   VIBRATIONAL SPECTROSCOPY AND CONFORMATION OF PEPTIDES, POLYPEPTIDES, AND PROTEINS [J].
KRIMM, S ;
BANDEKAR, J .
ADVANCES IN PROTEIN CHEMISTRY, 1986, 38 :181-364