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作 者:许倩[1,2] 石径[1] 黄和平[1] 罗永康[1]
机构地区:[1]中国农业大学食品科学与营养工程学院,北京100083 [2]塔里木大学南疆特色农产品深加工兵团重点实验室,新疆阿拉尔843300
出 处:《中国科技论文》2016年第6期633-637,共5页China Sciencepaper
基 金:高等学校博士学科点专项科研基金资助项目(20120008110020);国家自然科学基金资助项目(31171715)
摘 要:利用副干酪乳杆菌H9和植物乳杆菌P8菌株的粗酶液对浓缩乳蛋白在37℃下进行水解,并采用间接竞争酶联免疫吸附法(enzyme-linked immuno sorbent assay,ELISA)测定水解乳中α-乳白蛋白(α-LA)、β-乳球蛋白(β-LG)、α-酪蛋白(α-CN)和β-酪蛋白(β-CN)4种乳蛋白的抗原性与过敏原性,从而探讨2种乳酸杆菌粗酶液对浓缩乳蛋白的水解作用以及对乳蛋白抗原性及过敏原性的影响。结果表明:副干酪乳杆菌H9和植物乳杆菌P8菌株所产酶液在对浓缩乳蛋白进行水解的过程中,水解度逐渐增大,乳蛋白的抗原性及过敏原性在水解过程中都缓慢降低,抗原性的降低程度大于过敏原性的降低程度。其中效果最为显著的是副干酪乳杆菌H9和植物乳杆菌P8粗酶液水解后使β-LG抗原性分别降低了71.2%和63.1%;副干酪乳杆菌H9粗酶液水解后使α-LA、β-LG过敏原性分别降低了31.0%和41.2%。由此可见,不同菌种所产酶液对不同乳蛋白抗原性和过敏原性的影响有一定的差异。The hydrolysis role of enzyme produced from Lactobacillus paracasei H9 and L. plantarum P8 on the antigenicity and allergenicity of milk protein concentrates (MPC) was determined. MPC were digested at 37℃ by the crude enzyme of Lactobacillus, the antigenicity and allergenicity of α-lactalbumin (α-LA) , β-lactoglobulin (β-LG) , creasein (crCN) and β-casein (β-CN) in hydrolysates were measured by indirect competitive enzyme linked immunosorbent assay (ELISA) method. The results indicate that the hydrolysis degree increases gradually and the antigenicity and allergenicity of MPC reduces gradually during the enzymatic hydrolysis process. The reducing degree of milk proteins, antigenicity is higher than the degree of the allergenicity. After the crude enzyme hydrolysis of L. paracasei H9 and L. plantarum P8, the antigenicity of β-LG are decreased separately by 71. 2% and 63. 1%. Due to the hydrolysis of the crude enzyme of L. paracasei H9, the antigenicity of α-LA, β-LG are reduced by 31. 0% and 41. 2% respectively. The hydrolysis role of enzyme from different Lactobacillus strains on the antigenicity and allergenic-ity for four proteins is various.
关 键 词:乳加工 乳酸杆菌 粗酶液 浓缩乳蛋白 抗原性 过敏原性
分 类 号:TS252.1[轻工技术与工程—农产品加工及贮藏工程]
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