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首页> 外文期刊>Journal of Agricultural and Food Chemistry >Characterization of 'lettucine', a serine-like protease from Lactuca sativa leaves, as a novel enzyme for milk clotting
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Characterization of 'lettucine', a serine-like protease from Lactuca sativa leaves, as a novel enzyme for milk clotting

机译：来自莴苣叶的丝氨酸样蛋白酶“ lettucine”的表征，作为一种新型的凝乳酶

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摘要

In this work we focused on the characterization of a novel plant rennet purified from lettuce leaves (Lactuca sativa L. cv Romana). The lettuce protease, lettucine, showed trypsin-like, SV8-like, and caseinolytic activities. Although the enzyme did not recognize peptides having hydrophobic amino acid residues in the P, position of the target bond, it did show milk-clotting activity, suggesting that different bonds rather than the Phe(105)-Met(106) of the K-casein might be cleaved, still inducing milk-clotting. The enzyme exhibited proteolytic activity toward alpha-casein, beta-casein, kappa-casein, and milks with different fat contents, with the highest activity observed with partially skimmed milk, total casein, and alpha- and kappa-casein. SDS-PAGE studies showed that lettucine cleaved alpha-casein, beta-casein, and kappa-casein. In particular, we showed that a-casein breakdown occurred even though total casein or milks were supplied, suggesting that the lettuce enzyme is able to operate a significant disorganization of the casein's micellar structure. Moreover, the proteolytic activity of the enzyme analyzed under various technological parameters, such as temperature and pH, indicated that the lettuce enzyme is highly consistent with the milk-clotting process.
机译：在这项工作中，我们着重于从莴苣叶（莴苣（Lactuca sativa L. cv Romana））纯化的新型植物凝乳酶的表征。生菜蛋白酶lettucine具有胰蛋白酶样，SV8样和酪蛋白水解活性。尽管该酶无法识别在目标键的位置P上具有疏水性氨基酸残基的肽，但它确实显示出了牛奶凝结的活性，这表明该键不同于K-的Phe（105）-Met（106）酪蛋白可能会裂解，仍会导致牛奶凝结。该酶对α-酪蛋白，β-酪蛋白，κ-酪蛋白和脂肪含量不同的牛奶表现出蛋白水解活性，部分脱脂的牛奶，总酪蛋白以及α-酪蛋白和κ-酪蛋白的活性最高。 SDS-PAGE研究表明，lettucine裂解了α-酪蛋白，β-酪蛋白和kappa-酪蛋白。特别是，我们显示即使提供了总的酪蛋白或牛奶，α-酪蛋白也会发生分解，这表明莴苣酶能够使酪蛋白的胶束结构显着地分解。此外，在各种技术参数（例如温度和pH）下分析的酶的蛋白水解活性表明，莴苣酶与牛奶凝结过程高度一致。

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