Extraction and partial characterization of proteolytic activities from the cell surface of Lactobacillus helveticus Zuc2 |
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Authors: | Scolari G Vescovo M Zacconi C Vescovi F |
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Affiliation: | Istituto Microbiologia, Università Cattolica del Sacro Cuore (UCSC), via Emilia parmense, 84, 29100 Piacenza, Italy |
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Abstract: | Proteolytic activities were extracted from a dairy Lactobacillus helveticus strain and partially characterized. A first cell envelope proteinase (CEP) was extracted using a high ionic strength buffer, both in the presence and in the absence of Ca2+. Moreover, cell treatment by 5 M LiCl allowed for the selective removal of the S-layer protein and CEP, suggesting an enzyme ionic linkage to the cell envelope similar to that observed for the Slayer structure. The enzyme specificity against αs1-CN (f1-23) showed unusual activity on the Lys3-His4 bond compared with other proteinases of the same species. A second proteinase appeared to be linked to the cell membrane because it was extractable only after membrane disgregation by detergents. Its specificity against CN fractions and αs1-CN (f1-23) was different from that of the first CEP; moreover, the measured activity was lower than that of CEP. |
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Keywords: | Lactobacillus helveticus cell envelope proteinase specificity |
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