Abstract
This study compares N-glycosylation of two model enzymes, β-glucosidase and phosphatase, between wildtype yeast strains and heterologous hosts, Pichia pastoris and Schizosaccharomyces pombe. It also tries to correlate glycosylation differences to enzyme catalytic properties and to distinguish which part of glycosylation could be attributed to the nature of microorganism or to the glycoprotein itself (sequence, number of glycosylation sites...).
Highlights
Open AccessN-glycosylation differences between wild-type and recombinant strains affect catalytic properties of two model enzymes: β-glucosidase and phosphatase
Glycosylation is involved in many proteins' properties and functions such as conformation, thermostability, solubility, protection against proteolysis, intra-cellular migration, secretion
It tries to correlate glycosylation differences to enzyme catalytic properties and to distinguish which part of glycosylation could be attributed to the nature of microorganism or to the glycoprotein itself
Summary
N-glycosylation differences between wild-type and recombinant strains affect catalytic properties of two model enzymes: β-glucosidase and phosphatase. Address: Unité de Génie Enzymatique et Microbiologique, Agro.M – INRA, 2, place Viala, Montpellier, France, 34060 * Corresponding author from The 4th Recombinant Protein Production Meeting: a comparative view on host physiology Barcelona, Spain. 21–23 September 2006 Published: 10 October 2006 Microbial Cell Factories 2006, 5(Suppl 1):P35 doi:10.1186/1475-2859-5-S1-P35. The 4th Recombinant Protein Production Meeting: a comparative view on host physiology The organisers would like to thank Novozymes Delta Ltd who generously supported the meeting. Meeting abstracts – A single PDF containing all abstracts in this supplement is available here. http://www.biomedcentral.com/content/pdf/1475-2859-5-S1-info.pdf
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