Article Abstract:
The formation of alpha-galactosidase by Trichoderma reesei RUT C-30 and purification and characterization of the enzyme were described. Alpha-galactosidase was induced by alpha-galactosides and also by the monosaccharide galactose. The purified enzyme was a nonglycosylated monomer which had a molecular mass of 50 +/- 3 kDa and an isoelectric point of 5.2. The enzyme demonstrated moderate pH and thermal stabilities. It was active against several alpha-galactosides and galactomannan and was inhibited by the product galactose.
User Contributions:
Comment about this article or add new information about this topic:
Article Abstract:
Research was conducted to examine the role of endoproteolytic dibasis proprotein processing in the maturation of secretory proteins in Trichoderma reesei. A dibasic endopeptidase activity in T. reesei was demonstrated with the aid of an irreversible inhibitor (p-amidinophenylmethylsulfonyl fluoride (pAPMSF)). Results indicate the existence of various endoproteolytic proprotein processing enzymes in T. reesei and show that dibasic processing is necessary for the the secretion of the proproteins containing this target.
User Contributions:
Comment about this article or add new information about this topic:
Article Abstract:
The gene DPM1 of Saccharomyces cerevisiae was overexpressed in Trichoderma reesei to improve the fungus' protein secretion. This was done by encoding mannosylphosphodolichol synthase under homologous, constitutively acting expression signals. Research findings indicate that posttranscriptional processes lead to increased cellobiohydrolase I production. Electron microscopy of DPM1-amplified strains showed amorphous cell walls and over three times as many mitochondria as in the control.
User Contributions:
Comment about this article or add new information about this topic: