Effects of curdlan on the freeze-thaw stability of myosin gel

Authors

WANG Peisen, College of Food Science&Fujian Agriculture and Forestry University, Fuzhou, Fujian 350002, China; China-Ireland International Cooperation Laboratory of Foods Material Science and Structural Design, Fuzhou, Fujian 350002, China
LI Qianru, College of Food Science&Fujian Agriculture and Forestry University, Fuzhou, Fujian 350002, China; China-Ireland International Cooperation Laboratory of Foods Material Science and Structural Design, Fuzhou, Fujian 350002, China
JIANG Wentao, College of Food Science&Fujian Agriculture and Forestry University, Fuzhou, Fujian 350002, China; China-Ireland International Cooperation Laboratory of Foods Material Science and Structural Design, Fuzhou, Fujian 350002, China
MIAO Song, College of Food Science&Fujian Agriculture and Forestry University, Fuzhou, Fujian 350002, China; China-Ireland International Cooperation Laboratory of Foods Material Science and Structural Design, Fuzhou, Fujian 350002, China; Teagasc Food Research Centre, Moorepark, Fermoy, Co. Cork, Ireland
ZHANG Longtao, College of Food Science&Fujian Agriculture and Forestry University, Fuzhou, Fujian 350002, China; China-Ireland International Cooperation Laboratory of Foods Material Science and Structural Design, Fuzhou, Fujian 350002, China; Teagasc Food Research Centre, Moorepark, Fermoy, Co. Cork, Ireland
ZHENG Baodong, College of Food Science&Fujian Agriculture and Forestry University, Fuzhou, Fujian 350002, China; China-Ireland International Cooperation Laboratory of Foods Material Science and Structural Design, Fuzhou, Fujian 350002, China

Abstract

In order to investigate the effects and mechanization of curdlan on the free-thaw stability of surimi, gel strength and water holding capacity of myosin gel model in freeze-thaw cycles were observed. The intermolecular force, water distribution and microstructure were determined by LF-NMR, FT-IR and SEM respectively. The result showed that 1% curdlan increased the gel strength and water holding capacity and alleviated the reduction of gel strength and water holding capacity during freezing and thawing cycle. The addition of curdlan strengthened the hydrogen bonding inter myosin，which led to the formation of a compact three-dimensional network structure of myosin gel. Moreover, the liquidity of different components of water and the immobile water shifted into free water decreased, and the freeze-thaw stability and water holding capacity were increased.

Publication Date

5-28-2017

First Page

30

Last Page

34,53

DOI

10.13652/j.issn.1003-5788.2017.05.006

Recommended Citation

Peisen, WANG; Qianru, LI; Wentao, JIANG; Song, MIAO; Longtao, ZHANG; and Baodong, ZHENG (2017) "Effects of curdlan on the freeze-thaw stability of myosin gel," Food and Machinery: Vol. 33: Iss. 5, Article 6.
DOI: 10.13652/j.issn.1003-5788.2017.05.006
Available at: https://www.ifoodmm.cn/journal/vol33/iss5/6

References

[1] LI Xin-ke, XIA Wen-shui. Effects of chitosan on the gel properties of salt-soluble meat proteins from silver carp[J]. Carbohydrate Polymers, 2010, 82(3): 958-964.
[2] CHIN K B, GO M Y, XIONG You-ling. Konjac flour improved textural and water retention properties of transglutaminase-mediated, heat-induced porcine myofibrillar protein gel: Effect of salt level and transglutaminase incubation[J]. Meat Science, 2009, 81(3): 565-572.
[3] PATRASCU L, DOBRE I, ALEXE P. K-carrageenan effects on texture characteristics of meat emulsified sistems[J]. Studia Universitatis Babes-Bolyai Chemia, 2010, 55(3): 75-82.
[4] AYADI M A, KECHAOU A, MAKNI I, et al. Influence of carrageenan addition on turkey meat sausages properties[J]. Journal of Food Engineering, 2009, 93(3): 278-283.
[5] BS K, KIM J L J, IY L, et al. Curdlan gels as protein drug delivery vehicles[J]. Biotechnology Letters, 2000, 22(14): 1 127-1 130.
[6] FUNAMI T, YADA H, NAKAO Y. Thermal and rheological properties of curdlan gel in minced pork gel[J]. Food Hydrocolloids, 1998, 12(1): 55-64.
[7] 励慧敏, 杨柳. 大豆组织蛋白用于猪肉丸加工工艺优化[J]. 食品与机械, 2014, 30(4): 207-210.
[8] HU Ya-qin, LIU Wen-juan, YUAN Chun-hong, et al. Enhancement of the gelation properties of hairtail (Trichiurus haumela) muscle protein with curdlan and transglutaminase[J]. Food Chemistry, 2015, 176: 115-122.
[9] WU Chun-hua, YUAN Chun-hong, CHEN Shi-guo, et al. The effect of curdlan on the rheological properties of restructured ribbonfish (Trichiurus spp.) meat gel[J]. Food Chemistry, 2015, 179: 222-231.
[10] NISHITA K, KIMURA S, WATABE S. Structure-Function Relationships of Muscle Proteins from Fish and Shellfish[J]. Nihon-suisan-gakkai-shi, 1994, 60(4): 541-541.
[11] 周佺, 郭善广, 蒋爱民, 等. 肌肉盐溶蛋白热诱导凝胶特性研究进展[J]. 食品与机械, 2009, 25(3): 129-131.
[12] PARK J W, LANIER T C. Scanning Calorimetric Behavior of Tilapia Myosin and Actin due to Processing of Muscle and Protein Purification[J]. Journal of Food Science, 1989, 54(1):49-51.
[13] SHIROODI S G, RASCO B A, LO Y M. Influence of Xanthan-Curdlan Hydrogel Complex on Freeze-Thaw Stability and Rheological Properties of Whey Protein Isolate Gel over Multiple Freeze-Thaw Cycle[J]. Journal of Food Science, 2015(7): 1 498-1 505.
[14] LPEZ-DAZ J A, RODRGUEZ-ROMERO A, HERNN-DEZ-SANTOYO A, et al. Effects of Soy Glycinin Addition on the Conformation and Gel Strength of Two Pork Myosin Types[J]. Journal of Food Science, 2003, 68(9): 2 724-2 729.
[15] ZHOU Yan-zi, CHEN Cong-gui, CHEN Xing, et al. Contribution of three ionic types of polysaccharides to the thermal gelling properties of chicken breast myosin[J]. Journal of Agricultural & Food Chemistry, 2014, 62(12): 2 655-2 662.
[16] HUNT A, PARK J W. Alaska Pollock Fish Protein Gels as Affected by Refined Carrageenan and Various Salts[J]. Journal of Food Quality, 2013, 36(1): 51-58.
[17] MORENO H M, CARBALLO J, BORDERAS J. Application of response surface methodology to study the effect of different calcium sources in fish muscle-alginate restructured products[J]. Ciência E Tecnologia De Alimentos, 2011, 31(1): 209-216.
[18] 丁丽丽, 郭宏明, 吴俊, 等. 可得然胶在淡水鱼糜制品中的应用研究[J]. 食品工业科技, 2015, 36(17): 262-264.
[19] 肖旭华. 米渣及米渣蛋白对鲢鱼糜凝胶特性和冻融稳定性的影响[D]. 武汉: 华中农业大学, 2014: 60-61.
[20] QIN Hao, XU Peng, ZHOU Cun-liu, et al. Effects of l -Arginine on water holding capacity and texture of heat-induced gel of salt-soluble proteins from breast muscle[J]. Lebensmittel-Wissenschaft und-Technologie, 2015, 63(2): 912-918.
[21] GOETZ J, KOEHLER P. Study of the thermal denaturation of selected proteins of whey and egg by low resolution NMR[J]. LWT-Food Science and Technology, 2005, 38(5): 501-512.
[22] CARBONARO M, NUCARA A. Secondary structure of food proteins by Fourier transform spectroscopy in the mid-infrared region[J]. Amino Acids, 2010, 38(3): 679-690.
[23] PERISIC N, AFSETH N K, OFSTAD R, et al. Monitoring Protein Structural Changes and Hydration in Bovine Meat Tissue Due to Salt Substitutes by Fourier Transform Infrared (FTIR) Microspectroscopy[J]. Journal of Agricultural & Food Chemistry, 2011, 59(18): 10 052-10 061.
[24] ANDREEVA A E, KARAMANCHEVA I R. Insight into the secondary structure of chloramphenicol acetyltransferase type I : Computer analysis and FT-IR spectroscopic characterization of the protein structure[J]. Journal of Molecular Structure, 2001, 565-566(2): 177-182.
[25] BARTH A. Infrared spectroscopy of proteins[J]. Biochimica Et Biophysica Acta, 2007, 1 767(9): 1073-1 101.
[26] PEREZMATEOS M, MONTERO P. Contribution of hydrocolloids to gelling properties of blue whiting muscle[J]. European Food Research and Technology, 2000, 210(6): 383-390.
[27] HAN Min-yi, WANG Peng, XU Xing-lian, et al. Low-field NMR study of heat-induced gelation of pork myofibrillar proteins and its relationship with microstructural characteristics[J]. Food Research International, 2014, 62: 1 175-1 182.
[28] MA Fei, CHEN Cong-gui, ZHENG Lei, et al. Effect of high pressure processing on the gel properties of salt-soluble meat protein containing CaCl₂, and κ-carrageenan[J]. Meat Science, 2013, 95(1): 22-26.
[29] 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.