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首页> 外文期刊>International Dairy Journal >Natural diversity of aminotransferases and dehydrogenase activity in a large collection of Lactococcus lactis strains
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Natural diversity of aminotransferases and dehydrogenase activity in a large collection of Lactococcus lactis strains

机译：大量乳酸乳球菌菌株中氨基转移酶和脱氢酶活性的自然多样性

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摘要

The natural diversity of Lactococcus lactis was studied with respect to the flavour-generating enzymes leucine (Leu-AT) and aromatic (AraT) aminotransferase, and hydroxyisocaproic acid dehydrogenase (HicDH). The screening of 175 L. lactis strains required the development of enzyme assays to enable the use of high throughput screening facilities. Natural diversity was expressed as the difference between 10% of the strains with the highest and lowest enzyme activity. The natural diversity found for Leu-AT, AraT and HicDH activity was 13-, 49- and 30-fold, respectively. Leu-AT activity showed a weak correlation with the AraT and HicDH activity, whereas there was no correlation between AraT and HicDH activity. In the group of strains with the highest Leu-AT activity, 5- and 6-fold differences of AraT and HicDH activities were found, respectively. These results demonstrated that it is possible to select strains with specific combinations of important ripening enzymes that could enhance cheese flavour formation.
机译：乳酸乳球菌的自然多样性是针对产生香味的酶亮氨酸（Leu-AT）和芳香族（AraT）氨基转移酶，以及羟基异己酸脱氢酶（HicDH）进行的。筛选175株乳酸乳球菌菌株需要开发酶分析方法，以便能够使用高通量筛选设备。自然多样性表示为酶活性最高和最低的10％菌株之间的差异。发现的Leu-AT，AraT和HicDH活性的自然多样性分别为13倍，49倍和30倍。 Leu-AT活性显示与AraT和HicDH活性弱相关，而AraT和HicDH活性之间无相关性。在具有最高Leu-AT活性的菌株组中，分别发现AraT和HicDH活性的5倍和6倍差异。这些结果表明，可以选择具有重要成熟酶特定组合的菌株，这些酶可以增强奶酪的风味。

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