H
Helge Holo
Researcher at Norwegian University of Life Sciences
Publications - 80
Citations - 8340
Helge Holo is an academic researcher from Norwegian University of Life Sciences. The author has contributed to research in topics: Bacteriocin & Peptide sequence. The author has an hindex of 34, co-authored 78 publications receiving 7805 citations. Previous affiliations of Helge Holo include Vrije Universiteit Brussel.
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Journal ArticleDOI
High-Frequency Transformation, by Electroporation, of Lactococcus lactis subsp. cremoris Grown with Glycine in Osmotically Stabilized Media.
Helge Holo,Ingolf F. Nes +1 more
TL;DR: In this article, an efficient method for genetic transformation of lactococci by electroporation is presented, where highly competent cells for electrotransformation were obtained by growing cells in media containing high concentrations of glycine and 0.5 M sucrose as the osmotic stabilizers.
Journal ArticleDOI
Biosynthesis of bacteriocins in lactic acid bacteria
Ingolf F. Nes,Dzung B. Diep,Leiv Sigve Håvarstein,May Bente Brurberg,Vincent G. H. Eijsink,Helge Holo +5 more
TL;DR: The present review discusses recent findings concerning biosynthesis, genetics, and regulation of class II bacteriocins.
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Biochemical and genetic characterization of enterocin A from Enterococcus faecium, a new antilisterial bacteriocin in the pediocin family of bacteriocins.
Teresa Aymerich,Helge Holo,Leiv Sigve Håvarstein,Marta Hugas,Margarita Garriga,Ingolf F. Nes +5 more
TL;DR: A new bacteriocin has been isolated from an Enterococcus faecium strain and was purified to homogeneity as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, N-terminal amino acid sequencing, and mass spectrometry analysis.
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Lactococcin A, a new bacteriocin from Lactococcus lactis subsp. cremoris: isolation and characterization of the protein and its gene.
TL;DR: A new bacteriocin, termed lactococcin A (LCN-A), from Lactococcus lactis subsp.
Journal ArticleDOI
Enterocin B, a new bacteriocin from Enterococcus faecium T136 which can act synergistically with enterocin A.
TL;DR: The N-terminal amino acid sequences of enterocins A and B were determined, and the gene encoding enterocin B was sequenced as mentioned in this paper, and the primary translation product was a 71 aa peptide containing a leader peptide of the double-glycine type.