C
C Platteeuw
Publications - 7
Citations - 600
C Platteeuw is an academic researcher. The author has contributed to research in topics: Lactococcus lactis & Plasmid. The author has an hindex of 6, co-authored 7 publications receiving 584 citations.
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Journal ArticleDOI
Use of the Escherichia coli beta-glucuronidase (gusA) gene as a reporter gene for analyzing promoters in lactic acid bacteria.
C Platteeuw,G Simons,W.M. de Vos +2 more
TL;DR: This article corrects the article on p. 588 in vol.
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Food-grade cloning and expression system for Lactococcus lactis.
TL;DR: A versatile set of cloning and expression vectors has been developed for application in self-cloning and other genetic modifications of Lactococcus lactis, equipped with the controlled and strong lacA promoter of the lactococcal lactose operon.
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Metabolic engineering of Lactococcus lactis: influence of the overproduction of alpha-acetolactate synthase in strains deficient in lactate dehydrogenase as a function of culture conditions.
TL;DR: In this paper, the als gene for alpha-acetolactate synthase of Lactococcus lactis MG1363 was cloned on a multicopy plasmid under the control of the inducible L. lactis lacA promoter.
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Isolation and Characterization of the Hyperthermostable Serine Protease, Pyrolysin, and Its Gene from the Hyperthermophilic Archaeon Pyrococcus furiosus
W.G.B. Voorhorst,Rik I.L. Eggen,Ans C.M. Geerling,C Platteeuw,Roland J. Siezen,Willem M. de Vos +5 more
TL;DR: The archaeal pyrolysin showed highest homology with eucaryal tripeptidyl peptidases II on the amino acid level but a different cleavage specificity as shown by its endopeptidase activity toward caseins, casein fragments including αS1-casein and synthetic peptides.
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Location, characterization and expression of lytic enzyme-encoding gene, lytA, of Lactococcus lactis bacteriophage φ US3 †
C Platteeuw,Willem M. de Vos +1 more
TL;DR: Gene lytA, which encodes lytic enzyme (LytA), of the isometric Lactococcus lactis bacteriophage phi US3, was cloned and expressed in Escherichia coli and shows similarities to that of the autolysin of Streptococcus pneumoniae.