Properties and specificity of a cell-wall proteinase from Lactobacillus helveticus
Open accessAbstract
A cell-wall proteinase activity was extracted from cells of Lactobacillus helvetieus grown on MRS medium.The enzyme was characterized after DEAE-Trisacryl chrornatography and gel filtration on Ultrogel AcA 34 column.Two proteolytic fractions of different molecular weights were isolated.Their enzyme properties and specificity were clearly similar indicating that these fractions represented the same enzyme.It is a serine proteinase displaying optimum activity at pH 7.5-8.0and 42 oc.Peptide bonds cleaved in œs l and {3casein had no corn mon feature and no clear specificity can be defined.The six main peptides obtained after {3-casein hydrolysis were identified (Arg.-Leug,HisI06-PheI19, LYS'~6-GlnlSZ' ArglsrPhel9o, LeuI9,-Valzo9' TyrI93-VaIZ09) as weil as the two peptides liberated from œs l-casein (Arg.-Ileç,Arg.-Glus).These peptides whose size varies between 6 and 19 residues have probably to be hydrolysed by membrane-bound peptidases prior to their transport through the cytoplasmic membrane.Sorne of those released from the Cterminal part of {3-casein are potentially bitter.
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CEPs of L. helveticus are highly specific since the sites of cleavage on the caseins differ from one strain to another depending on the type of casein (α- or β-casein).
“CEPs of L. helveticus are highly specific since the sites of cleavage on the caseins differ from one strain to another depending on the type of casein (α- or β-casein) (Zevaco and Gripon, 1988; Jensen et al., 2009; Sadat-Mekmene et al., 2011a).”
From Lactobacillus helveticus: the proteolytic system (2013) · cites this paper as Zevaco and Gripon, 1988
CEPs of L. helveticus can cleave αs1- or β-casein at different sites not specifically related to one type of amino acid.
“Different studies have agreed that CEPs of L. helveticus can cleave αs1- or β-casein at different sites not specifically related to one type of amino acid (Zevaco and Gripon, 1988; Broadbent et al., 2011; Sadat-Mekmene et al., 2011b).”
From Lactobacillus helveticus: the proteolytic system (2013) · cites this paper as Zevaco and Gripon, 1988
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References 25 · Cited by 60
- Authors
- ZEVACO, C., & GRIPON, J.-C.
- Affiliations
- Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement (FR)
- Venue
- Le Lait
- Publisher
- EDP Sciences
- Published
- 1988
- Volume
- 68
- Issue
- 4
- Pages
- 393-407
- ISSN
- 0023-7302 (ISSN-L)
- OpenAlex
- W2164950053
- Cited by
- 60
- References
- 25
- Citations by year
- 2024: 1 · 2020: 1 · 2016: 1 · 2014: 1 · 2013: 3
- FWCI
- 5.59
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Le Lait (publishedVersion)
- HAL (submittedVersion, other-oa)
- HAL (submittedVersion)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
- Keywords
- Lactobacillus helveticus, serine protease, enzyme specificity, β-casein hydrolysis, proteolytic peptides, plasma membrane, bitter peptides, lactic acid bacteria
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