Publications by authors named "Pascal Viens"

Article Synopsis
  • The genome of Kitasatospora setae KM-6054 contains three chitosanase genes (csn1-3) that were cloned and expressed in Streptomyces lividans, resulting in the purification of four chitosanase enzymes.
  • The study found that the csn2 gene produces two distinct proteins, while Csn1 and Csn2H are typical GH46 chitosanases, and Csn3 is more similar to bacilli chitosanases.
  • The enzymes demonstrated various activities under different conditions, revealing significant biochemical diversity, and the findings provide insights into their structural characteristics through 3D modeling and sequence comparisons.
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Chitosanases, enzymes that catalyze the endo-hydrolysis of glycolytic links in chitosan, are the subject of numerous studies as biotechnological tools to generate low molecular weight chitosan (LMWC) or chitosan oligosaccharides (CHOS) from native, high molecular weight chitosan. Glycoside hydrolases belonging to family GH46 are among the best-studied chitosanases, with four crystallography-derived structures available and more than forty enzymes studied at the biochemical level. They were also subjected to numerous site-directed mutagenesis studies, unraveling the molecular mechanisms of hydrolysis.

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The csnR gene, localized at the beginning of an operon, csnR-K, which organization is conserved through many actinomycete genomes, was previously shown to repress the transcription of the chitosanase gene csnA in Streptomyces lividans. However, knowledge on the function of the whole csnR-K operon in the metabolism of chitosan (an N-deacetylated derivative of chitin) remained limited. Mutants of S.

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The agricultural sector is responsible for an important part of Canadian greenhouse gas (GHG) emissions, 8 % of the 747 Mt eq. CO(2) emitted each year. The pork industry, a key sector of the agrifood industry, has had a rapid growth in Canada since the middle 1980s.

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