组氨酸与氯化钾混合液对兔肉肌球蛋白特性的影响
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摘要
目的:研究组氨酸与氯化钾混合液对肌球蛋白溶出率、聚集特性和热凝胶特性的影响。方法:提取纯化兔腰大肌肌球蛋白,并用含有组氨酸的盐溶液透析处理,测定不同离子强度条件下蛋白溶出率、浊度以及热诱导凝胶的硬度和保水性(water holding capacity,WHC)。结果:经组氨酸处理后,在低离子强度(1 mmol/L KCl)条件下肌球蛋白的溶出率从17.2%提高到64.4%,聚集程度显著下降,热凝胶的硬度和保水性显著提高(P<0.05);而在生理离子强度(0.15 mol/L KCl)和高离子强度(0.6 mol/L KCl)条件下肌球蛋白的溶出率和聚集特性均未受组氨酸处理的影响,但其热凝胶硬度值显著降低(P<0.05);虽然在高离子强度条件下肌球蛋白热凝胶的保水性显著降低(P<0.05),但是在生理离子强度条件下凝胶保水性没有发生变化。结论:组氨酸处理可以显著增强低离子强度条件下肌球蛋白溶出率和其热凝胶形成能力,是低钠凝胶类肉制品生产和研发的一个新思路。
Objective: To study the combined effect of L-histidine and KCl on myosin solubility, aggregation and heatinduced gel properties. Methods: Rabbit Psoas major myosin was extracted and purified. After dialysis against different concentrations of KCl(1, 150 and 600 mmol/L) in the presence of L-histidine, it was measured for solubility, turbidity and heat-induced gel properties at different ionic strengths. Results: After L-histidine treatment, the solubility of rabbit meat myosin in a low ionic strength solution(1 mmol/L KCl) increased from 17.2% to 64.4%, and this is accompanied by a significant decrease in the extent of aggregation and a significant increase in the hardness and water-holding capacity(WHC) of heat-induced gels(P < 0.05). Nevertheless, at both physiological(0.15 mol/L KCl) and high ionic(0.6 mol/L KCl) strength, neither myosin solubility nor aggregation was affected by the presence of L-histidine in dialysis, although a significant decrease in the hardness of heat-induced gels was observed(P < 0.05). The WHC of heat-induced gels showed a significant reduction at high ionic strength, but exhibited no change at physiological ionic strength. Conclusion: L-histidine treatment can result in a significant increase in myosin solubility and heat-induced gel properties at low ionic strength conditions. This may provide new insights for developing low sodium gel-type meat products.
Objective: To study the combined effect of L-histidine and KCl on myosin solubility, aggregation and heatinduced gel properties. Methods: Rabbit Psoas major myosin was extracted and purified. After dialysis against different concentrations of KCl(1, 150 and 600 mmol/L) in the presence of L-histidine, it was measured for solubility, turbidity and heat-induced gel properties at different ionic strengths. Results: After L-histidine treatment, the solubility of rabbit meat myosin in a low ionic strength solution(1 mmol/L KCl) increased from 17.2% to 64.4%, and this is accompanied by a significant decrease in the extent of aggregation and a significant increase in the hardness and water-holding capacity(WHC) of heat-induced gels(P < 0.05). Nevertheless, at both physiological(0.15 mol/L KCl) and high ionic(0.6 mol/L KCl) strength, neither myosin solubility nor aggregation was affected by the presence of L-histidine in dialysis, although a significant decrease in the hardness of heat-induced gels was observed(P < 0.05). The WHC of heat-induced gels showed a significant reduction at high ionic strength, but exhibited no change at physiological ionic strength. Conclusion: L-histidine treatment can result in a significant increase in myosin solubility and heat-induced gel properties at low ionic strength conditions. This may provide new insights for developing low sodium gel-type meat products.
引文
[1]李继红,彭增起.温度、盐浓度和pH对盐溶蛋白质热诱导凝胶影响的研究[J].肉类工业,2004(4):39-41.
[2]费英,韩敏义,杨凌寒,等.pH对肌原纤维蛋白二级结构及其热诱导凝胶特性的影响[J].中国农业科学,2010,43(1):164-170.
[3]FUKUSHIMA H,SATOH Y,YOON S H,et al.Rheological properties of fast skeletal myosin rod and light meromyosin from walleye Pollack and white croaker:contribution of myosin fragments to thermal gel formation[J].Journal of Agricultural and Food Chemistry,2005,53(23):9193-9198.
[4]HIGUCHI T,OJIMA T,NISHITA K,et al.Heat-induced structural changes and aggregation of walleye Pollack myosin in the light meromyosin region[J].Fisheries Science,2002,68(5):1145-1150.
[5]WESTPHALEN A D,BRIGGS J L,LONERGAN S M,et al.Influence of muscle type on rheological properties of porcine myofibrillar protein during heat-induced gelation[J].Meat Science,2006,72:697-703.
[6]周光宏,徐幸莲,彭增起.肉品科学研究进展[J].中国农业科技导报,2006,8(3):1-10.
[7]LESIOW T,XIONG YoulingL.Chicken muscle homogenate gelation properties:effect of pH and muscle fiber type[J].Meat Science,2003,64(4):399-403.
[8]HAYAKAWA T,ITO T,WAKAMATSU J,et al.Myosin is solubilized in a neutral and low ionic strength solution containing L-histidine[J].Meat Science,2009,82:151-154.
[9]韩敏义,林丽军,徐幸莲,等.兔骨骼肌肌球蛋白溶液浊度和溶解度研究[J].南京农业大学学报,2003,26(4):93-96.
[10]徐幸莲,黄鸿兵,林丽军,等.蛋白质浓度、pH值、离子强度对兔骨骼肌肌球蛋白特凝胶特性的影响[J].江苏农业学报,2004,20(3):159-163.
[11]FENG Yuming,HULTIN H O.Effect of pH on the rheological and structural properties of gels of water-washed chicken-breast muscle at physiological ionic strength[J].Journal of Agricultural and Food Chemistry,2001,49(8):3927-3935.
[12]WANG Shufang,SMITH D M.Heat-induced denaturation and rheological properties of chicken breast myosin and F-actin in the presence and absence of pyrophosphate[J].Journal of Agricultural and Food Chemistry,1994,42(12):2665-2670.
[13]SUN Jingxin,WU Zhen,LI Ping,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.
[14]BALANGE A K,BENJAKUL S.Effect of oxidised tannic acid on the gel properties of mackerel(Rastrelliger kanagurta)mince and surimi prepared by different washing processes[J].Food Hydrocolloids,2009,23:1693-1701.
[15]HAYAKAWA T,ITO T,WAKAMATSU J,et al.Myosin filament depolymerizes in a low ionic strength solution containing L-histidine[J].Meat Science,2010,84,742-746.
[16]ITO Y,TATSUMI R,WAKAMATSU J,et al.The solubilization of myofibrillar proteins of vertebrate skeletal muscle in water[J].Animal Science Journal,2003,74:417-425.
[17]ZACHARY H,PARK J W.Rheological and biochemical characterization of salmon myosin as affected by constant heating rate[J].Journal of Agricultural and Food Chemistry,2011,76(2):343-349.
[18]杨龙江,南庆贤.肌肉蛋白质的热诱导凝胶特性及其及影响因素[J].肉类工业,2001(10):39-42.
[19]白云,钟国良,周光宏,等.蛋白浓度对兔腰大肌肌球蛋白热凝胶特性的影响[J].食品科学,2009,30(21):83-86.
[20]NOWSAD A A,KANOH S,NIWA E.Thermal gelation characteristics of breast and thigh muscles of spent hen and broiler and their surimi[J].Meat Science,2000,54:169-175.
[21]LEFEVRE F,FAUCONNEAU B.Thermal denaturation and aggregation properties of Atlantic Salmon myofibrils and myosin from white and red muscles[J].Journal of Agricultural and Food Chemistry,2007,55(12):4761-4770.
[22]韩敏义,费英,徐幸莲,等.低场NMR研究pH对肌原纤维蛋白热诱导凝胶的影响[J].中国农业科学,2009,42(6):2098-2104.
[23]BERTRAM H C,KRISTENSEN M,ANDERSEN H J.Functionality of myofibrillar proteins as affected by pH,ionic strength and heat treatment-a low-field NMR study[J].Meat Science,2004,68(2):249-256.
[24]LIU Ru,ZHAO Siming,XIE Bijun,et al.Contribution of protein conformation and intermolecular bonds to fish and pork gelation properties[J].Food Hydrocolloids,2011,25(5):898-906.
[25]LIU Ru,ZHAO Siming,LIU Yuanming,et al.Effect of pH on the gel properties and secondary structure of fish myosin[J].Food Chemistry,2010,121(1):196-202.
[26]XIA Xiufang,KONG Baohua,XIONG Youling,et al.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.
[27]KRISHNAMURTHY G,CHANG Haisheng,HERBERT O,et al.Solubility of chicken breast muscle proteins in solutions of low ionic strength[J].Journal of Agricultural and Food Chemistry,1996,44(2):408-415.
[2]费英,韩敏义,杨凌寒,等.pH对肌原纤维蛋白二级结构及其热诱导凝胶特性的影响[J].中国农业科学,2010,43(1):164-170.
[3]FUKUSHIMA H,SATOH Y,YOON S H,et al.Rheological properties of fast skeletal myosin rod and light meromyosin from walleye Pollack and white croaker:contribution of myosin fragments to thermal gel formation[J].Journal of Agricultural and Food Chemistry,2005,53(23):9193-9198.
[4]HIGUCHI T,OJIMA T,NISHITA K,et al.Heat-induced structural changes and aggregation of walleye Pollack myosin in the light meromyosin region[J].Fisheries Science,2002,68(5):1145-1150.
[5]WESTPHALEN A D,BRIGGS J L,LONERGAN S M,et al.Influence of muscle type on rheological properties of porcine myofibrillar protein during heat-induced gelation[J].Meat Science,2006,72:697-703.
[6]周光宏,徐幸莲,彭增起.肉品科学研究进展[J].中国农业科技导报,2006,8(3):1-10.
[7]LESIOW T,XIONG YoulingL.Chicken muscle homogenate gelation properties:effect of pH and muscle fiber type[J].Meat Science,2003,64(4):399-403.
[8]HAYAKAWA T,ITO T,WAKAMATSU J,et al.Myosin is solubilized in a neutral and low ionic strength solution containing L-histidine[J].Meat Science,2009,82:151-154.
[9]韩敏义,林丽军,徐幸莲,等.兔骨骼肌肌球蛋白溶液浊度和溶解度研究[J].南京农业大学学报,2003,26(4):93-96.
[10]徐幸莲,黄鸿兵,林丽军,等.蛋白质浓度、pH值、离子强度对兔骨骼肌肌球蛋白特凝胶特性的影响[J].江苏农业学报,2004,20(3):159-163.
[11]FENG Yuming,HULTIN H O.Effect of pH on the rheological and structural properties of gels of water-washed chicken-breast muscle at physiological ionic strength[J].Journal of Agricultural and Food Chemistry,2001,49(8):3927-3935.
[12]WANG Shufang,SMITH D M.Heat-induced denaturation and rheological properties of chicken breast myosin and F-actin in the presence and absence of pyrophosphate[J].Journal of Agricultural and Food Chemistry,1994,42(12):2665-2670.
[13]SUN Jingxin,WU Zhen,LI Ping,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.
[14]BALANGE A K,BENJAKUL S.Effect of oxidised tannic acid on the gel properties of mackerel(Rastrelliger kanagurta)mince and surimi prepared by different washing processes[J].Food Hydrocolloids,2009,23:1693-1701.
[15]HAYAKAWA T,ITO T,WAKAMATSU J,et al.Myosin filament depolymerizes in a low ionic strength solution containing L-histidine[J].Meat Science,2010,84,742-746.
[16]ITO Y,TATSUMI R,WAKAMATSU J,et al.The solubilization of myofibrillar proteins of vertebrate skeletal muscle in water[J].Animal Science Journal,2003,74:417-425.
[17]ZACHARY H,PARK J W.Rheological and biochemical characterization of salmon myosin as affected by constant heating rate[J].Journal of Agricultural and Food Chemistry,2011,76(2):343-349.
[18]杨龙江,南庆贤.肌肉蛋白质的热诱导凝胶特性及其及影响因素[J].肉类工业,2001(10):39-42.
[19]白云,钟国良,周光宏,等.蛋白浓度对兔腰大肌肌球蛋白热凝胶特性的影响[J].食品科学,2009,30(21):83-86.
[20]NOWSAD A A,KANOH S,NIWA E.Thermal gelation characteristics of breast and thigh muscles of spent hen and broiler and their surimi[J].Meat Science,2000,54:169-175.
[21]LEFEVRE F,FAUCONNEAU B.Thermal denaturation and aggregation properties of Atlantic Salmon myofibrils and myosin from white and red muscles[J].Journal of Agricultural and Food Chemistry,2007,55(12):4761-4770.
[22]韩敏义,费英,徐幸莲,等.低场NMR研究pH对肌原纤维蛋白热诱导凝胶的影响[J].中国农业科学,2009,42(6):2098-2104.
[23]BERTRAM H C,KRISTENSEN M,ANDERSEN H J.Functionality of myofibrillar proteins as affected by pH,ionic strength and heat treatment-a low-field NMR study[J].Meat Science,2004,68(2):249-256.
[24]LIU Ru,ZHAO Siming,XIE Bijun,et al.Contribution of protein conformation and intermolecular bonds to fish and pork gelation properties[J].Food Hydrocolloids,2011,25(5):898-906.
[25]LIU Ru,ZHAO Siming,LIU Yuanming,et al.Effect of pH on the gel properties and secondary structure of fish myosin[J].Food Chemistry,2010,121(1):196-202.
[26]XIA Xiufang,KONG Baohua,XIONG Youling,et al.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.
[27]KRISHNAMURTHY G,CHANG Haisheng,HERBERT O,et al.Solubility of chicken breast muscle proteins in solutions of low ionic strength[J].Journal of Agricultural and Food Chemistry,1996,44(2):408-415.