Specificity of the bound and free forms of the cell-envelope proteinase of Lactobacillus casei subsp. casei IFPL 731 towards the ?s1-casein-(1?23)-fragment

descriptionPublicationkeyboard_double_arrow_right Article 01 Dec 1997 English Publisher:Oxford University Press (OUP)Journal:Letters in Applied Microbiology, volume 25, pages 388-392 (issn: 0266-8254, eissn: 1365-2673,

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Authors: Fernández de Palencia, P.; Peláez, Carmen; Martín-Hernández, M. C.;

doi: 10.1111/j.1472-765x.1997.tb00002.x

handle: 10261/115777

Specificity of the bound and free forms of the cell-envelope proteinase of Lactobacillus casei subsp. casei IFPL 731 towards the ?s1-casein-(1?23)-fragment

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Abstract

The specificity of the bound and free forms of Lactobacillus casei subsp. casei IFPL 731 proteinase towards the α(s1)-casein-(1-23)-fragment has been studied. The use of the chelant agent EDTA for the extraction of the proteinase affects its specificity compared to either the use of lysozyme and mutanolysin or the whole-cell proteinase form. This gives a different pattern of the α(s1)-casein-fragment hydrolysis, as observed by HPLC. The effect of different chemical agents on the specific activity of the proteinase also varies depending on the method used to release the proteinase.

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Spanish National Research Council
Spain

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