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机构地区:[1]乳品科学教育部重点实验室,东北农业大学,黑龙江哈尔滨150030
出 处:《食品工业科技》2013年第10期187-191,共5页Science and Technology of Food Industry
基 金:教育部长江学者和创新团队发展计划项目(IRT0959);国家自然基金项目(31171717)
摘 要:以四株德氏乳杆菌保加利亚亚种为出发菌株,详细比较了四株菌产酸关键酶酶活的差异,从而找出菌株KLDS1.1006和KLDS1.1011后酸化较弱的主要原因及控制其产酸的关键酶。结果表明,H^+-ATPase可以控制菌株的能量代谢,是产酸关键酶;β-半乳糖苷酶对于分解乳糖产酸的贡献非常大,是乳糖代谢关键酶;乳酸脱氢酶和蛋白酶与后发酵产酸过程并没有必然联系;H^+-ATPase和β-半乳糖苷酶酶活性较弱是引起菌株KLDS1.1006和KLDS1.1011后酸化程度弱的根本原因。Four Lactobacillus delbrueckii subsp, bulgaricus studied the enzymes of metabolic pathway from lactose to strains were regarded as the research subject, lactic acid and H*-ATPase,to find which enzyme was the most important one that results in postacidification of yogurt,and the reason why KLDSI.1006 ang KLDS 1.1011 had a weak postacidification character. The key enzymes of Lactobacillus delbrueckii subsp. bulgaricus played important roles in producing lactic acid were l^-galactosidase and H ^-ATPase. Lactate dehydrogenase and protease showed no obvious correlation with postacidification. The enzyme activities of 6- galactosidase and H ATPase were weak,which was the fundamental reason why KLDSI.1006 and KLDS 1.1011 reflected weak postacidification.
关 键 词:德氏乳杆菌保加利亚亚种 H^+-ATPASE Β-半乳糖苷酶 乳酸脱氢酶 蛋白酶
分 类 号:TS201.3[轻工技术与工程—食品科学]
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