Extraction and partial characterization of proteolytic activities from the cell surface of Lactobacillus helveticus Zuc2

Scolari, G.; Vescovo, M.; Zacconi, C.; Vescovi, F.

doi:10.3168/jds.s0022-0302(06)72421-3

Cited by 37Probiotics and Fermented FoodsEnzyme Production and CharacterizationBacterial Genetics and Biotechnology

Extraction and partial characterization of proteolytic activities from the cell surface of Lactobacillus helveticus Zuc2

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Scolari, G., Vescovo, M., Zacconi, C., Vescovi, F.·2006·Journal of Dairy Science

DOI 10.3168/jds.s0022-0302(06)72421-3

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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 alpha(s1)-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 alpha(s1)-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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The CEPs of L. helveticus are also able to hydrolyze κ-casein and αs2-casein, although to a lesser extent than for the other caseins.
“The CEPs of L. helveticus are also able to hydrolyze κ-casein and αs2-casein; although to a lesser extent than for the other caseins (Ezzat et al., 1985; Yamamoto et al., 1998; Scolari et al., 2006; Jensen et al., 2009; Sadat-Mekmene et al., 2011a).”
From Lactobacillus helveticus: the proteolytic system (2013) · cites this paper as Scolari et al., 2006

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Authors: Scolari, G., Vescovo, M., Zacconi, C., & Vescovi, F.
Affiliations: Università Cattolica del Sacro Cuore (IT)
Corresponding author: Scolari, G.
ORCID: Vescovo, M.
Venue: Journal of Dairy Science
Publisher: American Dairy Science Association
Published: 2006-10
Volume: 89
Issue: 10
Pages: 3800-3809
ISSN: 0022-0302 (ISSN-L)
DOI: 10.3168/jds.s0022-0302(06)72421-3
OpenAlex: W1979083949
Cited by: 37
References: 37
Citations by year: 2026: 1 · 2025: 1 · 2024: 1 · 2023: 1 · 2022: 1 · 2021: 1 · 2020: 2 · 2019: 3 · 2018: 1 · 2017: 4 · 2016: 3 · 2014: 4 · 2013: 3 · 2012: 1
FWCI: 2.68
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 4490 d)
Locations: Journal of Dairy Science (publishedVersion)
PubMed (publishedVersion)
INFM-OAR (INFN Catania) (submittedVersion, other-oa)
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 › Genetics › Bacterial Genetics and Biotechnology
Keywords: Lactobacillus helveticus, proteolytic enzymes, cell envelope proteinase, S-layer proteins, αs1-casein, enzyme specificity, calcium dependence, dairy lactic acid bacteria, protein extraction
MeSH terms: Bacterial Proteins, Cell Fractionation, Chromatography, High Pressure Liquid, Hydrolysis, Membrane Proteins, Peptide Hydrolases, Substrate Specificity, Time Factors, Lithium Chloride, Lactobacillus helveticus

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Extraction and partial characterization of proteolytic activities from the cell surface of Lactobacillus helveticus Zuc2

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