Effect of different broken methods on gel structure of silver carpsurimi

Authors

WANG Lei, State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; National Center for Functional Food Engineering Technology Research, Jiangnan University, Wuxi, Jiangsu 214122, China; College of Food, Jiangnan Univers
FAN Daming, State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; National Center for Functional Food Engineering Technology Research, Jiangnan University, Wuxi, Jiangsu 214122, China; College of Food, Jiangnan Univers
HUANG Jianlian, Fujian Anjoy Food Share Co., Ltd., Xiamen, Fujian 361022, China
ZHAO Jianxin, State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; National Center for Functional Food Engineering Technology Research, Jiangnan University, Wuxi, Jiangsu 214122, China; College of Food, Jiangnan Univers
YAN Bowen, State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; National Center for Functional Food Engineering Technology Research, Jiangnan University, Wuxi, Jiangsu 214122, China; College of Food, Jiangnan Univers
ZHOU Wenguo, Fujian Anjoy Food Share Co., Ltd., Xiamen, Fujian 361022, China
ZHANG Wenhai, Fujian Anjoy Food Share Co., Ltd., Xiamen, Fujian 361022, China
ZHANG Hao, State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; National Center for Functional Food Engineering Technology Research, Jiangnan University, Wuxi, Jiangsu 214122, China; College of Food, Jiangnan Univers

Abstract

Compared with chopping method, the effect of stirring method on the gel properties of surimi products was studied. The results showed that this method of stirring-broken method increased the gel strength and water holding capacity of silver carp surimi, increased the hardness, adhesiveness, adhesiveness and chewiness, but had no effect on the whiteness. Under the conditions of 2% and 3% of salt addition, this kind of stirring-broken method had a significant effect on texture improvement of the surimi product, with the gel strength increasing by 70.2% and 66.7% respectively. The results of the content of salt-soluble protein, active sulfhydryl group, chemical reaction and turbidity of actomyosin showed that stirring-broken method increased the content of active sulfhydryl group, so that more sulfhydryl group oxidationed into disulfide bond to improve hydrophobic interactions, promoting the aggregation of protein molecules, resulting in increased turbidity of actomyosin, making the three-dimensional gel network more compact.

Publication Date

3-28-2018

First Page

32

Last Page

38

DOI

10.13652/j.issn.1003-5788.2018.03.007

Recommended Citation

Lei, WANG; Daming, FAN; Jianlian, HUANG; Jianxin, ZHAO; Bowen, YAN; Wenguo, ZHOU; Wenhai, ZHANG; and Hao, ZHANG (2018) "Effect of different broken methods on gel structure of silver carpsurimi," Food and Machinery: Vol. 34: Iss. 3, Article 7.
DOI: 10.13652/j.issn.1003-5788.2018.03.007
Available at: https://www.ifoodmm.cn/journal/vol34/iss3/7

References

[1] 李贤. 破碎方式对鱼糜凝胶特性的影响[D]. 武汉: 华中农业大学, 2014: 1-2.
[2] 吴汉民, 王海洪, 韩素珍, 等. 几种淡水鱼鱼糜特性的研究[J]. 食品科学学院, 1999, 20(9): 15-19.
[3] 陈申如, 刘阳, 李燕杰. 擂溃条件对鱼糜制品弹性的影响[J]. 大连工业大学学报, 2004, 23(3): 194-197.
[4] 刘海梅, 熊善柏, 谢笔钧, 等. 鲢鱼糜凝胶形成过程中化学作用力及蛋白质构象的变化[J]. 中国水产科学, 2008, 15(3): 469-475.
[5] 张磊. 淡水鱼方便食品斩拌设备的设计研究[D]. 南京: 河海大学, 2002: 2-5.
[6] 郑晓. 擂溃机杵头的运动及力学分析[J]. 武汉食品工业学院学报, 1996(4): 29-34.
[7] KONG Bao-hua, GUO Yuan-yuan, XIA Xiu-fang, et al. Cryoprotectants reduce protein oxidation and structure deterioration induced by freeze-thaw cycles in common carp (Cyprinus carpio) surimi[J]. Food Biophysics, 2013, 8(2): 104-111.
[8] ALVAREZ C, COUSO I, TEJADA M. Thermal gel degradation (modori) in sardine surimi gels[J]. Journal of Food Science, 1999, 64(4): 633-637.
[9] BENJAKUL S, VISESSANGUAN W. Transglutaminase-mediated setting in bigeye snapper Surimi[J]. Food Research International, 2003, 36(3): 253-266.
[10] 陈海华, 薛长湖. 钙盐溶液漂洗对竹荚鱼鱼糜凝胶特性的影响[J]. 食品与机械, 2009, 25(5): 5-9.
[11] 崔雁娜. 养殖大黄鱼蛋白质冷冻变性及抑制的研究[D]. 杭州: 浙江工商大学, 2009: 13-14.
[12] BALANGE A, BENJAKUL S. Enhancement of gel strength of bigeye snapper (Priacanthus tayenus) surimi using oxidised phenolic compounds[J]. Food Chemistry, 2009, 113(1): 61-70.
[13] BENJAKUL S, VISESSANGUAN W, SRIVILAI C. Porcine plasma protein as proteinase inhibitor in bigeye snapper (Priacanthus tayenus) muscle and surimi[J]. Journal of the Science of Food & Agriculture, 2001, 81(10): 1 039-1 046.
[14] KANG Zhuang-li, ZOU Yu-feng, XU Xing-lian, et al. Effect of a beating process, as a means of reducing salt content in Chinese-style meatballs (kung-wan): a physico-chemical and textural study[J]. Meat Science, 2014, 96(1): 147-152.
[15] LIAN P Z, LEE C M, HUFNAGEL L. Physicochemical properties of frozen red hake (Urophycis chuss) mince as affected by cryoprotective ingredients[J]. Journal of Food Science, 2000, 65(7): 1 117-1 123.
[16] CHEN Ching-san, HWANG D C, JIANG S T. Effect of storage temperatures on the formation of disulfides and denaturation of milkfish myosin (Chanos chanos)[J]. Journal of Food Science, 1988, 53(5): 1 333-1 335.
[17] GMEZ-GUILLN M C, BORDERIAS A J, MONTERO P. Chemical interactions of nonmuscle proteins in the network of sardine ( Sardina pilchardus ) muscle gels[J]. LWT-Food Science and Technology, 1997, 30(6): 602-608.
[18] 付湘晋, 许时婴, 王璋, 等. 酸碱处理对鲢鱼肌原纤维蛋白热变性、聚集、胶凝性质的影响[J]. 食品科学, 2008, 29(6): 100-103.
[19] 苏赵, 胡强, 李树红, 等. 海藻糖对草鱼鱼糜冻藏品质的影响[J]. 食品与机械, 2017, 33(7): 139-144.
[20] SAKAMOTO H, KUMAZAWA Y, TOIGUCHI S, et al. Gel strength enhancement by addition of microbial transglutaminase during onshore surimi manufacture[J]. Journal of Food Science, 1995, 60(2): 300-304.
[21] DESMOND E. Reducing salt: A challenge for the meat industry[J]. Meat Science, 2006, 74(1): 188-196.
[22] MAJUMDAR R K, SAHA A, DHAR B, et al. Effect of garlic extract on physical, oxidative and microbial changes during refrigerated storage of restructured product from Thai pangas (pangasianodon hypophthalmus) surimi[J]. Journal of Food Science & Technology, 2015, 52(12): 1-10.
[23] BADII F, HOWELL N K. A comparison of biochemical changes in cod (Gadus morhua) and haddock (Melanogrammus aeglefinus) fillets during frozen storage[J]. Journal of the Science of Food & Agriculture, 2002, 82(1): 87-97.
[24] 刘海梅. 鲢鱼糜凝胶及形成机理的研究[D]. 武汉: 华中农业大学, 2007: 1-5.
[25] DAVENPORT M P. Structure/function relationship of channel catfish (Ictalurus punctatus) muscle proteins subjected to ph-shift processing[J/OL]. [2017-11-02]. https://www.researchgate.net/publication/266039755_STRUCTUREFUNCTION_RELATIONSHIP_OF_CHANNEL_CATFISH_Ictalurus_punctatus_MUSCLE_PROTEINS_SUBJECTED_TO_pH-SHIFT_PROCESSING.
[26] POOWAKANJANA S, PARK J W. Biochemical characterisa-tion of Alaska pollock, Pacific whiting, and threadfin bream surimi as affected by comminution conditions[J]. Food Chemistry, 2013, 138(1): 200-207.
[27] KAMINER B, BELL A L. Myosin filamentogenesis: Effects of pH and ionic concentration[J]. Journal of Molecular Biology, 1966, 20(2): 391-401.
[28] 潘锦锋, 沈慧星, 尤娟, 等. 草鱼肌原纤维蛋白加热过程中理化特性的变化[J]. 中国农业大学学报, 2009, 14(6): 17-22.
[29] 周爱梅, 龚杰, 邢彩云, 等. 罗非鱼与鳙鱼鱼糜蛋白在冻藏中的生化及凝胶特性变化[J]. 华南农业大学学报, 2005, 26(3): 103-107.
[30] KO W C, YU Chi-cheng, HSU K C. Changes in conformation and sulfhydryl groups of tilapia actomyosin by thermal treatment[J]. LWT-Food Science and Technology, 2007, 40(8): 1 316-1 320.
[31] WAN J, KIMURA I, SATAKE M, et al. Effect of calcium ion concentration on the gelling properties and transglutaminase activity of walleye pollack surimi paste[J]. Fisheries Science, 1994, 60(1): 107-113.
[32] GILL T A, CONWAY J T. Thermal aggregation of cod (Gadus morhua) muscle proteins using l-ethyl-3-(3-dimethylaminopropyl) carbodiimide as a zero length cross-linker[J]. Journal of the Agricultural Chemical Society of Japan, 1989, 53(10): 2 553-2 562.
[33] WONNOP Visessanguan, MASAHIRO Ogawa, SHURYO Nakai A, et al. Physicochemical Changes and Mechanism of Heat-Induced Gelation of Arrowtooth Flounder Myosin[J]. Journal of Agricultural & Food Chemistry, 2000, 48(4): 1 016-1 023.