Hellio F C, Orange N, Guespin-Michel J F
Laboratoire de Microbiologie du Froid, Evreux, France.
Res Microbiol. 1993 Oct;144(8):617-25. doi: 10.1016/0923-2508(93)90064-9.
The psychotrophic strain Pseudomonas fluorescens MFO is known to express several enzymatic activities in milk, including extracellular proteolytic activity, optimally when cells are grown at 17.5 degrees C. In order to study the nature of the mechanisms controlling the production of the extracellular protease, we devised a defined medium in which this enzymatic activity was induced by an amino acid and small peptides. Regardless of the inducer, optimal proteolytic activity appeared at 17.5 degrees C. SDS-PAGE and isoelectrofocussing revealed a single protease produced by P. fluorescens MFO with all the inducers used and at all temperatures examined. The level of proteolytic activity correlated with the amount of enzyme in the supernatants.
嗜冷菌株荧光假单胞菌MFO已知在牛奶中表达多种酶活性,包括细胞外蛋白水解活性,当细胞在17.5摄氏度下生长时活性最佳。为了研究控制细胞外蛋白酶产生的机制的本质,我们设计了一种限定培养基,其中这种酶活性由氨基酸和小肽诱导。无论诱导剂如何,最佳蛋白水解活性都出现在17.5摄氏度。SDS-PAGE和等电聚焦显示,荧光假单胞菌MFO在使用的所有诱导剂和所有检测温度下都产生单一蛋白酶。蛋白水解活性水平与上清液中的酶量相关。