大目金枪鱼皮胶原明胶化过程中酸碱浓度对明胶理化性质的影响
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摘要
以大目金枪鱼皮为原料,考察了碱溶液浓度和酸溶液浓度对胶原明胶化的影响,研究表明,碱液质量分数为0.8%,酸溶液质量分数为2.0%时,明胶得率和凝胶强度均较优;傅里叶转换红外光谱(Fourier transform infrared spectroscopy,FTIR)结果表明,碱处理打破了胶原原有的氢键平衡,使三螺旋结构松散;不同质量分数的酸处理使得胶原原有的结构被破坏,三螺旋结构有所展开,二级结构向无序化转变,这些变化使热提胶过程中亚基更易释放;明胶化胶原的电镜扫描结果显示,碱处理可以对胶原蛋白的结构造成轻微的降解,继续进行酸处理过后,明胶化胶原降解程度明显,逐渐成无规则卷曲状,比较各处理组明胶化胶原表面结构状态后发现,碱处理质量分数为0.8%和酸处理质量分数为2.0%时,胶原表观破坏更明显,与得率结果一致;明胶电泳分析表明,碱处理质量分数较低时,明胶中高分子组分含量较低,而小分子组分含量较高于其他组,随着碱处理质量分数增加,明胶中α链含量增大,碱浓度至2.3%时,明胶中β链含量增高因而α链含量相对降低,导致凝胶强度降低。酸处理组中,质量分数在0.5%~1.5%范围内,酸处理质量分数在1.5%时,明胶中高分子质量组分较多,此时明胶凝胶强度最大。当酸处理质量分数高于2.0%后,所得明胶中的小分子组分含量逐渐增大,在酸处理质量分数达到2.5%后,明胶电泳条带中小分子组分的含量明显增加,造成凝胶强度逐渐降低。
The effect of alkali concentrations and acid concentration on yield and gel strength of gelatin from bigeye tuna were investigated. Besides,the effect of acid concentration and alkali concentration on the extracting process were studied by FTIR infrared spectroscopy,scanning electron microscopy(SEC)and SDS-PAGE. The tests tried to provide the theoretical basis for the control of the production parameters of tuna skin gelatin. The result showed that the optimal gelatin extraction condition was 0. 8% Na OH treatment and 2. 0% acetic acid treatment. The results of FTIR analysis showed that the intermolecular hydrogen bonds of the collagen were destroyed,while the intramolecular hydrogen bond enhanced after the alkali treatment. The breakage of the original hydrogen bond changed the structure of the collagen and the triple helix structure stretched. This made the subunit easily released during the gelatin extraction process. The acid treatment with different concentration made the original structure of collagen destroyed and the triple helix structure stretched. The content of random coil increased. The results of scanning electron microscopy showed that the alkali treatment could cause slight degradation of collagen structure merely. After the acid treatment,gelatinized collagen degradated obviously,and gradually become irregular curl. The damage of collagen was more obvious at 0. 8% alkali or 2. 0% acid treatment. The SDS-PAGE result showed that when concentration of alkali treatment was low,the content of high molecular weight components was lower while the content of small molecular weight was higher than other groups. Increasing the concentration of alkali gradually,the high molecular weight components increased. When the concentration of alkali treatment was increased to 2. 3%,the content of β-chain in gelatin increased and the content of α-chain decreased,which caused a decrease in gel strength. When acid was 0. 5%-1. 5%,especially at 1. 5%,the content of high molecular weight components was high and gel strength was high.When the acid concentration was higher than 2. 0%,the content of small weight molecule components in the gelatin was gradually increased. After the acid reached to 2. 5%,the intensity of the small molecule weight components of gelatin was significantly enhanced and caused gel strength gradually reduced.
The effect of alkali concentrations and acid concentration on yield and gel strength of gelatin from bigeye tuna were investigated. Besides,the effect of acid concentration and alkali concentration on the extracting process were studied by FTIR infrared spectroscopy,scanning electron microscopy(SEC)and SDS-PAGE. The tests tried to provide the theoretical basis for the control of the production parameters of tuna skin gelatin. The result showed that the optimal gelatin extraction condition was 0. 8% Na OH treatment and 2. 0% acetic acid treatment. The results of FTIR analysis showed that the intermolecular hydrogen bonds of the collagen were destroyed,while the intramolecular hydrogen bond enhanced after the alkali treatment. The breakage of the original hydrogen bond changed the structure of the collagen and the triple helix structure stretched. This made the subunit easily released during the gelatin extraction process. The acid treatment with different concentration made the original structure of collagen destroyed and the triple helix structure stretched. The content of random coil increased. The results of scanning electron microscopy showed that the alkali treatment could cause slight degradation of collagen structure merely. After the acid treatment,gelatinized collagen degradated obviously,and gradually become irregular curl. The damage of collagen was more obvious at 0. 8% alkali or 2. 0% acid treatment. The SDS-PAGE result showed that when concentration of alkali treatment was low,the content of high molecular weight components was lower while the content of small molecular weight was higher than other groups. Increasing the concentration of alkali gradually,the high molecular weight components increased. When the concentration of alkali treatment was increased to 2. 3%,the content of β-chain in gelatin increased and the content of α-chain decreased,which caused a decrease in gel strength. When acid was 0. 5%-1. 5%,especially at 1. 5%,the content of high molecular weight components was high and gel strength was high.When the acid concentration was higher than 2. 0%,the content of small weight molecule components in the gelatin was gradually increased. After the acid reached to 2. 5%,the intensity of the small molecule weight components of gelatin was significantly enhanced and caused gel strength gradually reduced.
引文
[1]周梦柔,马良,张宇昊.超高压诱导胶原蛋白明胶化机制研究进展[J].食品安全质量检测学报,2013(5):1 313-1 317.
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[3]周梦柔.猪皮胶原蛋白明胶化过程中的微观结构变化研究及明胶提取率明胶得率预测模型的构建[D].重庆:西南大学,2014.
[4]于玮.兔皮明胶的制备过程及其特性研究[D].重庆:西南大学,2016.
[5]CHO S M,GU Y S,KIM S B.Extracting optimization and physical properties of yellowfin tuna(Thunnus albacares)skin gelatin compared to mammalian gelatins[J].Food Hydrocolloids,2005,19(2):221-229.
[6]KARAYANNAKIDIS P D,CHATZIANTONIOU S E,ZOTOS A.Effects of selected process parameters on physical and sensorial properties of yellowfin tuna(Thunnus albacares)skin gelatin[J].Journal of Food Process Engineering,2014,37(5):461-473.
[7]GMEZ-ESTACA J,MONTERO P,FERNNDEZMARTN F,et al.Physico-chemical and film-forming properties of bovine-hide and tuna-skin gelatin:a comparative study[J].Journal of Food Engineering,2009,90(4):480-486.
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[9]叶小燕,曾少葵,余文国,等.罗非鱼皮营养成分分析及鱼皮明胶提取工艺的探讨[J].南方水产科学,2008,4(5):55-60.
[10]陈丽清,陈清,韩佳冬,等.猪皮超声波乳化脱脂工艺的研究[J].食品工业科技,2012,33(16):265-267.
[11]陈丽清,张宇昊,周梦柔,等.猪皮明胶提取过程中的超高压预处理工艺优化[J].农业工程学报,2012,28(19):262-269.
[12]位绍红,许永安.明胶提取工艺及其应用的研究进展[J].福建水产,2007(2):67-71.
[13]鲁军,陈海华.狭鳕鱼皮明胶提取工艺的研究[J].粮油加工,2009(11):140-142.
[14]NALINANON S,BENJAKUL S,VISESSANGUAN W,et al.Improvement of gelatin extraction from bigeye snapper skin using pepsin-aided process in combination with protease inhibitor[J].Food Hydrocolloids,2008,22(4):615-622.
[15]LIN C C,CHIOU T K,SUNG W C.Characteristics of gelatin from giant grouper(Epinephelus Lanceolatus)skin[J].International Journal of Food Properties,2015,18(11):2 339-2 348.
[16]MUYONGA J H,COLE C G B,DUODU K G.Fourier transform infrared(FTIR)spectroscopic study of acid soluble collagen and gelatin from skins and bones of young and adult Nile perch(Lates niloticus)[J].Food Chemistry,2004,86(3):325-332.
[17]朱欣星,安然,李昌朋,等.胶原与明胶的结构研究:方法,结果与分析[J].皮革科学与工程,2012,22(5):9-14.
[18]HE L,MU C,SHI J,et al.Modification of collagen with a natural cross-linker,procyanidin[J].International Journal of Biological Macromolecules,2011,48(2):354-359.
[19]KITTIPHATTANABAWON P,BENJAKUL S,SINTHUSAMRAN S,et al.Gelatin from clown featherback skin:Extraction conditions[J].LWT-Food Science and Technology,2016,66:186-192.
[20]石燕,刘凡,葛辉,等.微胶囊形成过程中蛋白质二级结构变化的红外光谱分析[J].光谱学与光谱分析,2012,32(7):1 815-1 819.
[21]LEDWARD D A.Gelation of gelatin[J].Functional Properties of Food Macromolecules,1986:171-201.
[22]SIMS T J,BAILEY A J,FIELDT D S.The chemical basis of molecular weight differences in gelatins[J].The Imaging Science Journal,1997,45(3/4):171-177.
[23]SEE S F,GHASSEM M,MAMOT S,et al.Effect of different pretreatments on functional properties of African catfish(Clarias gariepinus)skin gelatin[J].Journal of Food Science and Technology,2015,52(2):753-762.
[2]赵格,康阳妃,刘津宁,等.胶原明胶化程度快速评价体系构建分析与展望[J].食品工业科技,2015,36(5):370-374.
[3]周梦柔.猪皮胶原蛋白明胶化过程中的微观结构变化研究及明胶提取率明胶得率预测模型的构建[D].重庆:西南大学,2014.
[4]于玮.兔皮明胶的制备过程及其特性研究[D].重庆:西南大学,2016.
[5]CHO S M,GU Y S,KIM S B.Extracting optimization and physical properties of yellowfin tuna(Thunnus albacares)skin gelatin compared to mammalian gelatins[J].Food Hydrocolloids,2005,19(2):221-229.
[6]KARAYANNAKIDIS P D,CHATZIANTONIOU S E,ZOTOS A.Effects of selected process parameters on physical and sensorial properties of yellowfin tuna(Thunnus albacares)skin gelatin[J].Journal of Food Process Engineering,2014,37(5):461-473.
[7]GMEZ-ESTACA J,MONTERO P,FERNNDEZMARTN F,et al.Physico-chemical and film-forming properties of bovine-hide and tuna-skin gelatin:a comparative study[J].Journal of Food Engineering,2009,90(4):480-486.
[8]崔利锋,许柳雄.世界大洋性渔业概况[M].北京:海洋出版社,2011.
[9]叶小燕,曾少葵,余文国,等.罗非鱼皮营养成分分析及鱼皮明胶提取工艺的探讨[J].南方水产科学,2008,4(5):55-60.
[10]陈丽清,陈清,韩佳冬,等.猪皮超声波乳化脱脂工艺的研究[J].食品工业科技,2012,33(16):265-267.
[11]陈丽清,张宇昊,周梦柔,等.猪皮明胶提取过程中的超高压预处理工艺优化[J].农业工程学报,2012,28(19):262-269.
[12]位绍红,许永安.明胶提取工艺及其应用的研究进展[J].福建水产,2007(2):67-71.
[13]鲁军,陈海华.狭鳕鱼皮明胶提取工艺的研究[J].粮油加工,2009(11):140-142.
[14]NALINANON S,BENJAKUL S,VISESSANGUAN W,et al.Improvement of gelatin extraction from bigeye snapper skin using pepsin-aided process in combination with protease inhibitor[J].Food Hydrocolloids,2008,22(4):615-622.
[15]LIN C C,CHIOU T K,SUNG W C.Characteristics of gelatin from giant grouper(Epinephelus Lanceolatus)skin[J].International Journal of Food Properties,2015,18(11):2 339-2 348.
[16]MUYONGA J H,COLE C G B,DUODU K G.Fourier transform infrared(FTIR)spectroscopic study of acid soluble collagen and gelatin from skins and bones of young and adult Nile perch(Lates niloticus)[J].Food Chemistry,2004,86(3):325-332.
[17]朱欣星,安然,李昌朋,等.胶原与明胶的结构研究:方法,结果与分析[J].皮革科学与工程,2012,22(5):9-14.
[18]HE L,MU C,SHI J,et al.Modification of collagen with a natural cross-linker,procyanidin[J].International Journal of Biological Macromolecules,2011,48(2):354-359.
[19]KITTIPHATTANABAWON P,BENJAKUL S,SINTHUSAMRAN S,et al.Gelatin from clown featherback skin:Extraction conditions[J].LWT-Food Science and Technology,2016,66:186-192.
[20]石燕,刘凡,葛辉,等.微胶囊形成过程中蛋白质二级结构变化的红外光谱分析[J].光谱学与光谱分析,2012,32(7):1 815-1 819.
[21]LEDWARD D A.Gelation of gelatin[J].Functional Properties of Food Macromolecules,1986:171-201.
[22]SIMS T J,BAILEY A J,FIELDT D S.The chemical basis of molecular weight differences in gelatins[J].The Imaging Science Journal,1997,45(3/4):171-177.
[23]SEE S F,GHASSEM M,MAMOT S,et al.Effect of different pretreatments on functional properties of African catfish(Clarias gariepinus)skin gelatin[J].Journal of Food Science and Technology,2015,52(2):753-762.