Jan Wery
DSM
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Featured researches published by Jan Wery.
Bioresource Technology | 2010
Stefan Kühnel; S.W.A. Hinz; Laurice Pouvreau; Jan Wery; Henk A. Schols; Harry Gruppen
The filamentous fungus Chrysosporium lucknowense (C1) is a rich source of cell wall degrading enzymes. In the present paper four arabinose releasing enzymes from C1 were characterized, among them one endoarabinanase, two arabinofuranosidases and one exoarabinanase. Combinations of these enzymes released up to 80% of the arabinose present in sugar beet arabinan to fermentable monosugars. Besides the main product arabinobiose, unknown arabinose oligomers are produced from highly branched arabinan when endoarabinanase was combined with exoarabinanase and/or arabinofuranosidase. All described arabinose releasing enzymes are temperature stable up to 50 degrees C and have a broad pH stability. This makes C1 arabinohydrolases suitable for many biotechnical applications, like co-fermentation bioethanol production.
Yeast | 1997
Jan C. Verdoes; Jan Wery; Teun Boekhout; Albert J. J. van Ooyen
The glyceraldehyde‐3‐phosphate dehydrogenase (GPD; EC1.2.1.12)‐encoding gene (gpd) was isolated from a genomic library of Phaffia rhodozyma CBS 6938. Unlike some other eukaryotic organisms the gpd gene is represented by a single copy in P. rhodozyma. The complete nucleotide sequence of the coding, as well as the flanking non‐coding regions was determined. The nucleotide sequence of gpd predicted six introns and a polypeptide chain of 339 amino acids. The codon usage in the gpd gene of P. rhodozyma was highly biased and was significantly different from the codon usage in other yeasts. Phylogenetic analysis of different yeasts and filamentous asco‐ and basidiomycetes gpd sequences indicated that the gpd gene of P. rhodozyma forms a cluster with the corresponding genes of filamentous basidiomycetes.
Biotechnology Techniques | 1998
Jan Wery; Jan C. Verdoes; A. J. J. Van Ooyen
An efficient transformation system for the astaxanthin-producing yeast Phaffia rhodozyma was developed based on electroporation that routinely yields approximately 1000 transformants per μg of plasmid DNA. The high transformation efficiency depends on vector integration in the ribosomal DNA (rDNA) and the presence of the homologous glycolytic glyceraldehyde-3-phosphate dehydrogenase (gpd) promoter and terminator to drive the expression of the transposon Tn5 encoded kanamycin resistance gene (KmR) as a selective marker. Using this system stable transformants were obtained, carrying multiple plasmid copies. Plasmid copy number could be markedly increased by deletion of the gpd terminator from the transforming plasmid.
Bioresource Technology | 2012
Gleb S. Dotsenko; O. A. Sinitsyna; S.W.A. Hinz; Jan Wery; A. P. Sinitsyn
The Bxl5-gene encoding a GH3 glycoside hydrolase of Chrysosporium lucknowense C1 was successfully cloned, the homologous recombinant product was secreted, purified and characterized. Bxl5 (120 ± 5 kDa) was able to hydrolyze low molecular weight substrates and polysaccharides containing β-glucosidic as well as β-xylosidic residues. The K(m) and V(max)/E values were found to be 0.3mM and 88 s(-1) on p-nitrophenyl-β-d-glucopyranoside (PNPG), and 13.5mM and 1.8s(-1) on p-nitrophenyl-β-d-xylopyranoside (PNPX). Optimal pH and temperature for Bxl5 were 4.6 and 75°C for the PNPG hydrolysis, and 5.0-5.5 and 70°C for PNPX hydrolysis. The enzyme was quite stable when incubated at elevated temperatures up to 65°C. Bxl5 hydrolyzes polymeric β-glucans by the exo-mechanism allowing their complete conversion to d-glucose and is effective for xylan hydrolysis in combination with endo-acting xylan-degrading enzymes. The enzyme seems to be a very promising for bioconversion purposes.
Annual Review of Microbiology | 2011
Peter J. Punt; Anthony Levasseur; Hans Visser; Jan Wery; Eric Record
For more than a century, filamentous fungi have been used for the production of a wide variety of endogenous enzymes of industrial interest. More recently, with the use of genetic engineering tools developed for these organisms, this use has expanded for the production of nonnative heterologous proteins. In this review, an overview is given of examples describing the production of a special class of these proteins, namely chimeric proteins. The production of two types of chimeric proteins have been explored: (a) proteins grafted for a specific substrate-binding domain and (b) fusion proteins containing two separate enzymatic activities. Various application areas for the use of these chimeric proteins are described.
Industrial Biotechnology | 2011
Hans Visser; Vivi Joosten; Peter J. Punt; Alexander V. Gusakov; Phil T. Olson; Rob Joosten; Jeffrey Bartels; Jaap Visser; A. P. Sinitsyn; Mark Aaron Emalfarb; Jan C. Verdoes; Jan Wery
Gene | 1997
Jan Wery; D.A.M. Gutker; A.C.H.M. Renniers; Jan C. Verdoes; A. van Ooyen
Journal of Cereal Science | 2009
Sandra W. A. Hinz; Laurice Pouvreau; Rob Joosten; Jeffrey Bartels; Meliana C. Jonathan; Jan Wery; Henk A. Schols
Archive | 2010
Peter J. Punt; Richard P. Burlingame; Christine Marie Pynnonen; Phillip T. Olson; Jan Wery; Johannes Heinrich Visser; Mark Aaron Emalfarb; Jacob Visser; Jan Cormelis Verdoes
Archive | 1996
Albert Johannes Joseph Van Ooijen; Jan Cornelis Verdoes; Jan Wery