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Release and partial characterization of cell-envelope proteinases from Lactococcus lactis subsp. lactis IFPL 359 and Lactobacillus casei subsp. casei IFPL 731 isolated from raw goat,s-milk cheese

AutorFernández de Palencia, P. ; Peláez, Carmen ; Requena, Teresa ; Martín-Hernández, M. C.
Fecha de publicación1995
CitaciónZeitschrift fur Lebensmittel -Untersuchung und -Forschung 201: 87- 90 (1995)
ResumenDifferent methods of releasing the cell-envelope proteinase (CEP) from Lactococcus lactis IFPL 359 (Lc-CEP) and Lactobacillus casei IFPL 731 (Lb-CEP) have been tested. Release of Lc-CEP was higher in Ca2+-free buffer than in the presence of lysozyme and Ca2+-. Lb-CEP was not soluble in Ca2+--free buffer, making necessary the use of chelating agents such as ethylenediaminetetraacetate (EDTA) to attain release yields of 15-20%. Solubilizing the cell wall of lb. casei using lysozyme and mutanolysin improved CEP release yields, even in the presence of Ca2+-. Two differently charged chromophoric peptides were degraded by whole cells and the soluble fractions studied at different hydrolysis rates in both the strains considered. Based on the specificity of these CEPs for the different substrates, the two proteinases can be placed in the same class as the CEPI/III mixed-type variants that have been identified in lactococcal proteinases. In both strains ß-casein was hydrolysed more rapidly than αs-cascin. © 1995 Springer-Verlag.
Identificadoresdoi: 10.1007/BF01193207
issn: 0044-3026
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