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Diversity in proteinase specificity of thermophilic lactobacilli as revealed by hydrolysis of dairy and vegetable proteins

机译:乳和植物蛋白水解显示嗜热乳杆菌蛋白酶特异性的多样性

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Ability of industrially relevant species of thermophilic lactobacilli strains to hydrolyze proteins from animal (caseins and β-lactoglobulin) and vegetable (soybean and wheat) sources, as well as influence of peptide content of growth medium on cell envelope-associated proteinase (CEP) activity, was evaluated. Lactobacillus delbrueckii subsp. lactis (CRL 581 and 654), L. delbrueckii subsp. bulgaricus (CRL 454 and 656), Lactobacillus acidophilus (CRL 636 and 1063), and Lactobacillus helveticus (CRL 1062 and 1177) were grown in a chemically defined medium supplemented or not with 1 % Casitone. All strains hydrolyzed mainly β-casein, while degradation of αs-caseins was strain dependent. Contrariwise, κ-Casein was poorly degraded by the studied lactobacilli. β-Lactoglobulin was mainly hydrolyzed by CRL 656, CRL 636, and CRL 1062 strains. The L. delbrueckii subsp. lactis strains, L. delbrueckii subsp. bulgaricus CRL 656, and L. helveticus CRL 1177 degraded gliadins in high extent, while the L. acidophilus and L. helveticus strains highly hydrolyzed soy proteins. Proteinase production was inhibited by Casitone, the most affected being the L. delbrueckii subsp. lactis species. This study highlights the importance of proteolytic diversity of lactobacilli for rational strain selection when formulating hydrolyzed dairy or vegetable food products.
机译:工业相关嗜热乳酸菌菌株具有水解动物(酪蛋白和β-乳球蛋白)和植物(大豆和小麦)来源的蛋白质的能力,以及生长培养基的肽含量对细胞膜结合蛋白酶(CEP)活性的影响,进行了评估。德氏乳杆菌亚种。乳酸(CRL 581和654),L.delbrueckii亚种保加利亚(CRL 454和656),嗜酸乳杆菌(CRL 636和1063)和瑞士乳杆菌(CRL 1062和1177)在添加或不添加1%Casitone的化学成分确定的培养基中生长。所有菌株主要水解β-酪蛋白,而αs-酪蛋白的降解是依赖菌株的。相反,所研究的乳酸杆菌对κ-酪蛋白的降解较弱。 β-乳球蛋白主要被CRL 656,CRL 636和CRL 1062菌株水解。 L. delbrueckii亚种。乳酸菌,德氏乳杆菌亚种。保加利亚CRL 656和瑞士乳杆菌CRL 1177高度降解麦醇溶蛋白,而嗜酸乳杆菌和瑞士乳杆菌菌株高度水解大豆蛋白。蛋白酶的产生被Casitone抑制,受影响最大的是L. delbrueckii亚种。乳酸菌种。这项研究强调了在配制水解乳制品或蔬菜食品时,乳杆菌蛋白水解多样性对于合理选择菌株的重要性。

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