Purification and characterization of intracellular proteinase from Lactobacillus casei ssp. casei LLG
In: Journal of dairy science, Jg. 87 (2004), Heft 12, S. 4097-4103
Online
academicJournal
- print, 42 ref
Zugriff:
The intracellular proteinase of Lactobacillus casei ssp. casei LLG was isolated in the cytoplasmic fraction with 0.05 M Tris-HCl buffer (pH 7.5). The enzyme was purified by the fast protein liquid chromatography system equipped with ion-exchange and gel filtration chromatographies. This proteinase comprised a single monomeric form and had a molecular weight of about 55 kDa and an isoelectric point near pH 4.9. The optimum pH and temperature for the enzyme activity were determined to be pH 6.5 and 37°C, respectively. The enzyme was inactivated by metal-chelating compounds (EDTA, 1,10-phenanthroline) and less affected by serine proteinase inhibitors (diisopropylfluorophosphate, phenyl-methylsulfonyl fluoride). Proteinase activity was increased by Ca++, Mn++, and Co++, and inhibited by Cu++, Mg++, and Zn++. The activity of this enzyme to hydrolyze casein appeared to be more active on β-casein than αs1-casein and κ-casein as monitored by polyacrylamide gel electrophoresis.
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Purification and characterization of intracellular proteinase from Lactobacillus casei ssp. casei LLG
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Autor/in / Beteiligte Person: | SHIN, J. Y ; JEON, W. M ; KIM, G.-B ; LEE, B. H |
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Zeitschrift: | Journal of dairy science, Jg. 87 (2004), Heft 12, S. 4097-4103 |
Veröffentlichung: | Savoy, IL: American Dairy Science Association, 2004 |
Medientyp: | academicJournal |
Umfang: | print, 42 ref |
ISSN: | 0022-0302 (print) |
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