Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Harry Laan"'
Publikováno v:
International Dairy Journal. 8:267-274
The effects of pH, NaCl and CaCl2 concentration on aminopeptidase activities of lactic acid bacteria were investigated in order to assess the potential role of these enzymes on proteolysis during cheese ripening. A NaCl concentration of around 4% and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::61c1a1e72ea8f163f8e41d96a0b5e55b
https://doi.org/10.1016/s0958-6946(98)00054-5
https://doi.org/10.1016/s0958-6946(98)00054-5
Publikováno v:
Acta Biotechnologica. 13:95-101
The synthesis of extracellular serine proteinase of Lactococcus lactis was studied during the growth in a batch and a continuous culture on chemically defined media. In a batch culture the proteinase synthesis started during the exponential phase of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::87d07d90f8bbcd8e109bf81088c7ba39
https://doi.org/10.1002/abio.370130202
https://doi.org/10.1002/abio.370130202
Autor:
Harry Laan, Wil N. Konings
Publikováno v:
Applied and Environmental Microbiology. 57:2586-2590
The molecular masses of purified extracellular serine proteinase of a number of Lactococcus lactis strains vary significantly, and these molecular mass values do not correspond to the values estimated on the basis of genetic data. The discrepancies c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65263458bae474f516d1eae2124c7019
https://doi.org/10.1128/aem.57.9.2586-2590.1991
https://doi.org/10.1128/aem.57.9.2586-2590.1991
Publikováno v:
The Journal of dairy research. 63(2)
SummaryMonoclonal antibodies against peptidases ofLactococcus lactiswere isolated and characterized: PEPN1–4 against a lysyl aminopeptidase PepN, PEPT1–5 against a tripeptidase PepT and PEPD1–3 against a dipeptidase PepD. These monoclonal antib
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b6fb0027d69ece332fb9e783cfcea91
https://pubmed.ncbi.nlm.nih.gov/8861346
https://pubmed.ncbi.nlm.nih.gov/8861346
Autor:
V. Juillard, Harry Laan, Wn Konings, C. M. Jeronimus-Stratingh, A. P. Bruins, Edmund R.S. Kunji
Publikováno v:
Journal of Bacteriology
Journal of Bacteriology, American Society for Microbiology, 1995, 177 (12), pp.3472-3478
Journal of Bacteriology, American Society for Microbiology, 1995, 177 (12), pp.3472-3478
The peptides released from beta-casein by the action of PI-type proteinase (PrtP) from Lactococcus lactis subsp. cremoris Wg2 have been identified by on-line coupling of liquid chromatography to mass spectrometry. After 24 h of incubation of beta-cas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64550f7928b630c50e699477f64b471b
https://hal.inrae.fr/hal-02713849
https://hal.inrae.fr/hal-02713849
Publikováno v:
Applied and environmental microbiology, 57(7), 1899-1904. AMER SOC MICROBIOLOGY
Activity of the lactococcal cell envelope-located serine proteinase depends on the presence of membrane-associated lipoprotein PrtM. To differentiate between the action of the proteinase and the action of PrtM in the process of proteinase maturation,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2247cd8431e8c21371996362116fdc0b
https://europepmc.org/articles/PMC183497/
https://europepmc.org/articles/PMC183497/
Autor:
Harry Laan, Wil N. Konings
Publikováno v:
Applied and Environmental Microbiology. 55:3101-3106
The procedure generally used for the isolation of extracellular, cell-associated proteinases of Lactococcus lactis species is based on the release of the proteinases by repeated incubation and washing of the cells in a Ca 2+ -free buffer. For L. lact
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db316def45a2e50bc1e39416e031c188
https://doi.org/10.1128/aem.55.12.3101-3106.1989
https://doi.org/10.1128/aem.55.12.3101-3106.1989
Publikováno v:
Applied and environmental microbiology, 54(1), 239-244. AMER SOC MICROBIOLOGY
The Streptococcus cremoris Wg2 proteinase gene, cloned in S. lactis, specified a proteinase which exhibited the same specificity toward casein as did the proteinase isolated from the original host. Although the cloned gene lacked the last 130 codons,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::254140357a15909274dc7387b6471c0e
https://research.rug.nl/en/publications/5bac65e6-9e0c-4f9d-a9d2-e04581ce6a36
https://research.rug.nl/en/publications/5bac65e6-9e0c-4f9d-a9d2-e04581ce6a36
proteinase ofLactococcus lactis subsp. cremoris Wg2 were isolated after immunization ofBALB/cmicewitha partially purified preparation ofthe proteinase. Themonoclonal antibodies reacted withthe126-kilodalton proteinase bandina Western immunoblot. Allb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e269e6e2122e607679ecf4679503ec71
https://europepmc.org/articles/PMC202844/
https://europepmc.org/articles/PMC202844/
Autor:
Wn Konings, Alfred J. Haandrikman, Aat M. Ledeboer, Harry Laan, Gerhardus Venema, Jan Kok, S Soemitro
Publikováno v:
Journal of Bacteriology, 171(5), 2789-2794. AMER SOC MICROBIOLOGY
Directly upstream of the Lactococcus lactis subsp. cremoris Wg2 proteinase gene is an oppositely directed open reading frame (ORF1). The complete nucleotide sequence of ORF1, encoding a 33-kilodalton protein, was determined. A protein of approximatel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b149982aeb921a636869034ee2165ed
https://europepmc.org/articles/PMC209965/
https://europepmc.org/articles/PMC209965/