海参低温处理品质与理化性质研究
|
摘要
以新鲜海参为原料,20℃低温处理,考察海参在不同处理时间(0,1/24,1/4,1/2,1,2,3,4,5,6 d)下品质和理化性质变化。结果表明,随着低温热处理时间的延长,可溶性胶原的含量随时间的延长呈上升趋势,6 d时含量为0 d的3.23倍;硬度和咀嚼度在1/4 d后都发生急剧下降,最后其硬度和咀嚼度仅为0 d状态下的0.92%和0.22%;SDS-PAGE结果表明,分子质量为200.0 ku和44.3 ku的肌动蛋白条带随着热处理时间的延长发生明显的蛋白降解;与0 d相比,组织蛋白酶-L活力在1/2 d时增加1.6倍,caspase-3活力在1 d时增加3倍,随后随着处理时间的延长而下降;ESR结果表明,在20℃低温热处理1/2 d,海参自由基信号强度达到最高水平,是0 d的1.67倍。综上所述,在20℃低温热处理下,海参体内自由基生成,氧化促进组织蛋白酶-L和caspase-3被激活,进而导致蛋白质降解,胶原溶出,最终影响海参的品质。
In this study,sea cucumbers were as raw materials,treated at low temperature of 20 ℃,studying on the quality and physicochemical properties of sea cucumber under different treatment conditions at 0,1/24,1/4,1,2,3,4,5 and 6 d.The study found that the soluble collagen amount increased with the prolongation of time at low-temperature treatment and the content of soluble collagen of 6 d is 3.23 times of 0 d.The hardness and chewiness dramatically decreased after 1/4 d and the hardness and chewiness are only 0.92% and 0.22% of the state of 0 d.SDS-PAGE result indicated that the notable proteolysis happened to the protein with molecular weight of 200 ku and 44 ku of actin with the heating time extension.Compared with the control group,the activity of cathepsin-L and caspase-3 was increased 1.6 times at 1/2 d and 3 times at 1 d and their activity decreases with the prolongation of time at low-temperature treatment.ESR results indicated that the free radicals production of sea cucumber reached the highest level after 1/2 d and compared with 0 d,its value increased by 1.67 times.In summary,at 20 ℃ low temperature heat treatment,free radicals in sea cucumbers were generated and oxidation promotes cathepsin-L and caspase-3 activation,which leaded to degradation of protein,dissolution of collagen,and ultimately morphological and quality changes in sea cucumber.
In this study,sea cucumbers were as raw materials,treated at low temperature of 20 ℃,studying on the quality and physicochemical properties of sea cucumber under different treatment conditions at 0,1/24,1/4,1,2,3,4,5 and 6 d.The study found that the soluble collagen amount increased with the prolongation of time at low-temperature treatment and the content of soluble collagen of 6 d is 3.23 times of 0 d.The hardness and chewiness dramatically decreased after 1/4 d and the hardness and chewiness are only 0.92% and 0.22% of the state of 0 d.SDS-PAGE result indicated that the notable proteolysis happened to the protein with molecular weight of 200 ku and 44 ku of actin with the heating time extension.Compared with the control group,the activity of cathepsin-L and caspase-3 was increased 1.6 times at 1/2 d and 3 times at 1 d and their activity decreases with the prolongation of time at low-temperature treatment.ESR results indicated that the free radicals production of sea cucumber reached the highest level after 1/2 d and compared with 0 d,its value increased by 1.67 times.In summary,at 20 ℃ low temperature heat treatment,free radicals in sea cucumbers were generated and oxidation promotes cathepsin-L and caspase-3 activation,which leaded to degradation of protein,dissolution of collagen,and ultimately morphological and quality changes in sea cucumber.
引文
[1]农业部渔业局.2017年中国渔业统计年鉴[M].北京:中国农业出版社,2018:23.
[2]QI H,FU H,DONG X,et al.Apoptosis induction is involved in UVA-induced autolysis in sea cucumber Stichopus japonicus[J].Journal of Photochemistry&Photobiology B Biology,2016,158:130-135.
[3]傅卉,张警予,赵欣涛,等.刺参体壁超氧化物歧化酶提取及酶学性质的研究[J].食品科技,2015(9):150-154.
[4]方允中,郑荣梁.自由基生物学的理论与应用[M]北京:科学出版社,2002:872-932.
[5]奚倩,董秀芳,李楠,等.紫外线诱导刺参自溶氧化损伤及体内抗氧化应答[J].现代食品科技,2015,31(9):74-80.
[6]QI H,DONG X F,ZHAO Y P,et al.ROS production in homogenate from the body wall of sea cucumber Stichopus japonicus under UVA irradiation:ESR spin-trapping study[J].Food Chemistry,2016,192:358.
[7]李楠,冯丁丁,赵雅娉,等.基于ESR技术检测水产品加工过程中的氧化物质[J].中国食品学报,2017,17(2):256-263.
[8]FONTANESI L,SPERONI C,BUTTAZZONI L,et al.Association between cathepsin L(CTSL)and cathepsin S(CTSS)polymorphisms and meat production and carcass traits in Italian Large White pigs[J].Meat Science,2010,85(2):331-338.
[9]CH魪RETA R,DELBARRE-LADRAT C,DE LAM-BALLERIE-ANLON M,el al.Calpain and cathepsin activities in post mortem fish and meat muscles[J].Food Chemistry,2007,101(4):1474-1479.
[10]ZHU B,DONG X,SUN L,et al.Effect of thermal treatment on the texture and microstructure of abalone muscle(Haliotis discus)[J].Food Science and Biotechnology,2011,20(6):1467-1473.
[11]STARKEY C P,GEESINK G H,ODDY V H,et al.Explaining the variation in lamb longissimus,shear force across and within ageing periods using protein degradation,sarcomere length and collagen characteristics[J].Meat Science,2015,105:32-37.
[12]王凤林,阎佳楠,唐越,等.热处理中海参和鱼皮胶原变化的对比研究[J].中国食品学报,2016,16(12):86-92.
[13]郑明静,周美龄,陈妮,等.超高压处理对海参组织结构及品质影响的研究[J].食品工业科技,2016,37(4):187-191,210.
[14]CHRISTENSEN L,ERTBJERG P,AASLYNG M D,et al.Effect of prolonged heat treatment from 48℃to 63℃on toughness,cooking loss and color of pork[J].Meat Science,2011,88(2):280-285.
[15]WICHULADA T,NANTIPA P,KUNIHIKO KThermal denaturation profiles of catfish and tilapia myofibrils as affected by pH for heating[J].Fisheries Science,2012,78(2):431-439.
[16]LADRAT.In vitro proteolysis of myofibrillar and sarcoplasmic proteins of white muscle of sea bass(Dicentrarchus labrax L.):effects of cathepsins B,D and L[J].Food Chemistry,2003,81(4):517-525.
[17]GE L H,XU Y,XIA W.The function of endogenous cathepsin in quality deterioration of grass carp(Ctenopharyngodon idella)fillets stored in chilling conditions[J].International Journal of Food Science&Technology,2015,50(3):797-803.
[18]KEMP C M,KING D A,SHACKELFORD S D,et al.The caspase proteolytic system in callipyge and normal lambs in longissimus,semimembranosus,and infraspinatus muscles during postmortem storage[J].Journal of Animal Science,2009,87(9):2943-2951.
[19]CAO J X,OU C R,ZOU Y F,et al.Activation of caspase-3 and its correlation with shear force in bovine skeletal muscles during postmortem conditioning[J].Journal of Animal Science,2013,91(9):4547-4552.
[20]ADAMS-CIOABA M A,KRUPA J C,XU C,et al Structural basis for the recognition and cleavage of histone H3 by cathepsin L[J].Nature Communications,2011,2(1):197-205.
[21]ACHARYA A,DAS I,CHANDHOK D,et al.Redox regulation in cancer:a double-edged sword with therapeutic potential[J].Oxidative Medicine&Cellular Longevity,2010,3(1):23-34.
[2]QI H,FU H,DONG X,et al.Apoptosis induction is involved in UVA-induced autolysis in sea cucumber Stichopus japonicus[J].Journal of Photochemistry&Photobiology B Biology,2016,158:130-135.
[3]傅卉,张警予,赵欣涛,等.刺参体壁超氧化物歧化酶提取及酶学性质的研究[J].食品科技,2015(9):150-154.
[4]方允中,郑荣梁.自由基生物学的理论与应用[M]北京:科学出版社,2002:872-932.
[5]奚倩,董秀芳,李楠,等.紫外线诱导刺参自溶氧化损伤及体内抗氧化应答[J].现代食品科技,2015,31(9):74-80.
[6]QI H,DONG X F,ZHAO Y P,et al.ROS production in homogenate from the body wall of sea cucumber Stichopus japonicus under UVA irradiation:ESR spin-trapping study[J].Food Chemistry,2016,192:358.
[7]李楠,冯丁丁,赵雅娉,等.基于ESR技术检测水产品加工过程中的氧化物质[J].中国食品学报,2017,17(2):256-263.
[8]FONTANESI L,SPERONI C,BUTTAZZONI L,et al.Association between cathepsin L(CTSL)and cathepsin S(CTSS)polymorphisms and meat production and carcass traits in Italian Large White pigs[J].Meat Science,2010,85(2):331-338.
[9]CH魪RETA R,DELBARRE-LADRAT C,DE LAM-BALLERIE-ANLON M,el al.Calpain and cathepsin activities in post mortem fish and meat muscles[J].Food Chemistry,2007,101(4):1474-1479.
[10]ZHU B,DONG X,SUN L,et al.Effect of thermal treatment on the texture and microstructure of abalone muscle(Haliotis discus)[J].Food Science and Biotechnology,2011,20(6):1467-1473.
[11]STARKEY C P,GEESINK G H,ODDY V H,et al.Explaining the variation in lamb longissimus,shear force across and within ageing periods using protein degradation,sarcomere length and collagen characteristics[J].Meat Science,2015,105:32-37.
[12]王凤林,阎佳楠,唐越,等.热处理中海参和鱼皮胶原变化的对比研究[J].中国食品学报,2016,16(12):86-92.
[13]郑明静,周美龄,陈妮,等.超高压处理对海参组织结构及品质影响的研究[J].食品工业科技,2016,37(4):187-191,210.
[14]CHRISTENSEN L,ERTBJERG P,AASLYNG M D,et al.Effect of prolonged heat treatment from 48℃to 63℃on toughness,cooking loss and color of pork[J].Meat Science,2011,88(2):280-285.
[15]WICHULADA T,NANTIPA P,KUNIHIKO KThermal denaturation profiles of catfish and tilapia myofibrils as affected by pH for heating[J].Fisheries Science,2012,78(2):431-439.
[16]LADRAT.In vitro proteolysis of myofibrillar and sarcoplasmic proteins of white muscle of sea bass(Dicentrarchus labrax L.):effects of cathepsins B,D and L[J].Food Chemistry,2003,81(4):517-525.
[17]GE L H,XU Y,XIA W.The function of endogenous cathepsin in quality deterioration of grass carp(Ctenopharyngodon idella)fillets stored in chilling conditions[J].International Journal of Food Science&Technology,2015,50(3):797-803.
[18]KEMP C M,KING D A,SHACKELFORD S D,et al.The caspase proteolytic system in callipyge and normal lambs in longissimus,semimembranosus,and infraspinatus muscles during postmortem storage[J].Journal of Animal Science,2009,87(9):2943-2951.
[19]CAO J X,OU C R,ZOU Y F,et al.Activation of caspase-3 and its correlation with shear force in bovine skeletal muscles during postmortem conditioning[J].Journal of Animal Science,2013,91(9):4547-4552.
[20]ADAMS-CIOABA M A,KRUPA J C,XU C,et al Structural basis for the recognition and cleavage of histone H3 by cathepsin L[J].Nature Communications,2011,2(1):197-205.
[21]ACHARYA A,DAS I,CHANDHOK D,et al.Redox regulation in cancer:a double-edged sword with therapeutic potential[J].Oxidative Medicine&Cellular Longevity,2010,3(1):23-34.