低温冻藏对肌原纤维蛋白凝胶特性的影响
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摘要
研究了冻藏温度(-5,-18,-26,-35,-70℃)和冻藏时间(1,3,6,12个月)对猪肉肌原纤维蛋白溶解性、浊度和凝胶特性(白度值、保水性、流变学特性、微观结构)的影响。结果表明:冻藏后肌原纤维特性发生明显变化,且差异显著(P<0.05)。冻藏后肌原纤维蛋白的溶解性降低,浊度增加,蛋白凝胶持水性、白度值、硬度、弹性、黏性、回弹性和流变学参数G′值均显著降低,且冻藏时间越长、冻藏温度越高变化越显著。凝胶扫描电镜图表明:冻藏后肌原纤维蛋白凝胶三维网状结构被破坏。
Effect of the freezing storage temperature(-5,-18,-26,-35 ℃ and-70 ℃) and time(0, 1, 3, 6,9, 12 months) on the solubility, turbidity, gel properties(whiteness, water-holding capacity, rheological property, microstructure) of porcine myofibrilla protein were studied. Changes in properties of myofibrilla protein were found, and the difference is significant(P<0.05). The decrease in solubility, water holding capacity, whiteness, hardness, rheology parameter(G′) of myofibril protein and the increase in turbidity of myofibrillar protein were induced by freezing storage temperature and time. The longer storage time and the higher storage temperature were, the more significant change in protein property was. The result of gel microstructure showed: the three-dimensional reticular structure of myofibrillar protein gel was destroyed after freezing storage.
Effect of the freezing storage temperature(-5,-18,-26,-35 ℃ and-70 ℃) and time(0, 1, 3, 6,9, 12 months) on the solubility, turbidity, gel properties(whiteness, water-holding capacity, rheological property, microstructure) of porcine myofibrilla protein were studied. Changes in properties of myofibrilla protein were found, and the difference is significant(P<0.05). The decrease in solubility, water holding capacity, whiteness, hardness, rheology parameter(G′) of myofibril protein and the increase in turbidity of myofibrillar protein were induced by freezing storage temperature and time. The longer storage time and the higher storage temperature were, the more significant change in protein property was. The result of gel microstructure showed: the three-dimensional reticular structure of myofibrillar protein gel was destroyed after freezing storage.
引文
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[2] OZEK N S, BAL I B, YILDIRIM S, et al. Structural and functional characterization of simvastatininduced myotoxicity in different skeletal muscles[J].Biochimica et Biophysica Acta(BBA)-General Subjects, 2014, 1840(1):406-415.
[3] LEYGONIE C, BRITZ T J, HOFFMAN L C. Impact of freezing and thawing on the quality of meat[J]. Meat Science, 2012, 91(2):93-98.
[4] NI N, WANG Z Y, HE F, et al. Gel properties and molecular forces of lamb myofibrillar protein during heat induction at different p H values[J]. Process Biochemistry, 2014, 49(4):631-636.
[5] JIANG J, XIONG Y L. Extreme pH treatments enhance the structure-reinforcement role of soy protein isolate and its emulsions in pork myofibrillar protein gels in the presence of microbial transglutaminase[J].Meat Science, 2013, 93(3):469-476.
[6] HAYAKAWA T, YOSHIDA Y, YASUI M. Heat-induced gelation of myosin in a low ionic strength so lution containing L-histidine[J]. Meat Science, 2012,90(1):77-80.
[7] LIN S B, CHEN L C, CHEN H H. The change of thermal gelation properties of horse mackerel mince led by protein denaturation occurring in frozen storage and consequential air floatation wash[J]. Food Research International, 2005, 38(1):19-27.
[8] BENJAKUL S, CHANARAT S. Effect of formaldehyde on protein cross-linking and gel forming ability of surimi from lizardfish induced by microbial trans glutaminase[J]. Food Hydrocolloids, 2013, 30(2):704-711.
[9] XIA X F, KONG B H. Decreased gelling and emulsifying properties of myofibrillar protein from repeatedly frozen-thawed porcine longissimus muscle are due to protein denaturation and susceptibility to aggregation[J]. Meat Science, 2010, 85(3):481-486.
[10] SAELEAW T, BENJAKUL S. Physico-chemical properties and fishy odour of gelatin from seabass(Lates calcarifer)skin stored in ice[J]. Food Bioscience, 2015, 10(1):59-68.
[11] XIA X F, KONG B H, LIU J, et al. Influence of different thawing methods on physicochemical changes and protein oxidation of porcine longissimus muscle[J]. LWT-Food Science and Technology, 2012,46(1):280-286.
[12] BENJAKUL S, BAHER F. Physicochmical and enzymatic changes of Cod muscle proteins subjected to different freeze-thaw cycles[J]. Journal of the Science of Food and Agriculture, 2000, 80(8):1143-1150.
[13] BENJAKUL S, VISESSANGUAN W, ISHIZAKI S,et al. Differences in gelation characteristics of natural actomyosin from two species of bigeye smapper,Priacanthus tayenus and Priacanthus macracanthus[J]. Journal of Food Science, 2001, 66(9):1311-1318.
[14] SUN J X, WU Z, XU X L, et al. Effect of peanut protein isolate on functional properties of chicken salt-soluble proteins from breast and thigh muscles during heat-induced gelation[J]. Meat Science, 2012,91(1):88-92.
[15] ROMOTOWSKA P E, GUDJONSDOTTIR M, KRISTINSDOTTIR T B, et al. Effect of brining and frozen storage on physicochemical properties of well-fed Atlantic mackerel(Scomber scombrus)intended for hot smoking and canning[J]. LWT-Food Science and Technology, 2016, 72(10):199-205
[16] WESTPHALEN A D, BRIGGS J L, LONERGAN S M. Influence of muscle type on rheological properties of porcine myofibrillar proteins during heat-induced gelatio[J]. Meat Science, 2006, 72(4):697-703.
[17] PARK D, XIONG Y L, ALDERTONAND A L, et al. Biochemical changes in myofibrillar protein isolates exposed to three oxidizing systems[J]. Journal of Agriculture and Food Chemistry, 2006, 54(12):4445-4451.
[2] OZEK N S, BAL I B, YILDIRIM S, et al. Structural and functional characterization of simvastatininduced myotoxicity in different skeletal muscles[J].Biochimica et Biophysica Acta(BBA)-General Subjects, 2014, 1840(1):406-415.
[3] LEYGONIE C, BRITZ T J, HOFFMAN L C. Impact of freezing and thawing on the quality of meat[J]. Meat Science, 2012, 91(2):93-98.
[4] NI N, WANG Z Y, HE F, et al. Gel properties and molecular forces of lamb myofibrillar protein during heat induction at different p H values[J]. Process Biochemistry, 2014, 49(4):631-636.
[5] JIANG J, XIONG Y L. Extreme pH treatments enhance the structure-reinforcement role of soy protein isolate and its emulsions in pork myofibrillar protein gels in the presence of microbial transglutaminase[J].Meat Science, 2013, 93(3):469-476.
[6] HAYAKAWA T, YOSHIDA Y, YASUI M. Heat-induced gelation of myosin in a low ionic strength so lution containing L-histidine[J]. Meat Science, 2012,90(1):77-80.
[7] LIN S B, CHEN L C, CHEN H H. The change of thermal gelation properties of horse mackerel mince led by protein denaturation occurring in frozen storage and consequential air floatation wash[J]. Food Research International, 2005, 38(1):19-27.
[8] BENJAKUL S, CHANARAT S. Effect of formaldehyde on protein cross-linking and gel forming ability of surimi from lizardfish induced by microbial trans glutaminase[J]. Food Hydrocolloids, 2013, 30(2):704-711.
[9] XIA X F, KONG B H. Decreased gelling and emulsifying properties of myofibrillar protein from repeatedly frozen-thawed porcine longissimus muscle are due to protein denaturation and susceptibility to aggregation[J]. Meat Science, 2010, 85(3):481-486.
[10] SAELEAW T, BENJAKUL S. Physico-chemical properties and fishy odour of gelatin from seabass(Lates calcarifer)skin stored in ice[J]. Food Bioscience, 2015, 10(1):59-68.
[11] XIA X F, KONG B H, LIU J, et al. Influence of different thawing methods on physicochemical changes and protein oxidation of porcine longissimus muscle[J]. LWT-Food Science and Technology, 2012,46(1):280-286.
[12] BENJAKUL S, BAHER F. Physicochmical and enzymatic changes of Cod muscle proteins subjected to different freeze-thaw cycles[J]. Journal of the Science of Food and Agriculture, 2000, 80(8):1143-1150.
[13] BENJAKUL S, VISESSANGUAN W, ISHIZAKI S,et al. Differences in gelation characteristics of natural actomyosin from two species of bigeye smapper,Priacanthus tayenus and Priacanthus macracanthus[J]. Journal of Food Science, 2001, 66(9):1311-1318.
[14] SUN J X, WU Z, XU X L, et al. Effect of peanut protein isolate on functional properties of chicken salt-soluble proteins from breast and thigh muscles during heat-induced gelation[J]. Meat Science, 2012,91(1):88-92.
[15] ROMOTOWSKA P E, GUDJONSDOTTIR M, KRISTINSDOTTIR T B, et al. Effect of brining and frozen storage on physicochemical properties of well-fed Atlantic mackerel(Scomber scombrus)intended for hot smoking and canning[J]. LWT-Food Science and Technology, 2016, 72(10):199-205
[16] WESTPHALEN A D, BRIGGS J L, LONERGAN S M. Influence of muscle type on rheological properties of porcine myofibrillar proteins during heat-induced gelatio[J]. Meat Science, 2006, 72(4):697-703.
[17] PARK D, XIONG Y L, ALDERTONAND A L, et al. Biochemical changes in myofibrillar protein isolates exposed to three oxidizing systems[J]. Journal of Agriculture and Food Chemistry, 2006, 54(12):4445-4451.