Topic
Pichia pastoris
About: Pichia pastoris is a research topic. Over the lifetime, 7937 publications have been published within this topic receiving 162645 citations. The topic is also known as: Komagataella pastoris.
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TL;DR: The aim of the study was the identification, cloning and disruption of the GAS1 homologue of Pichia pastoris, a glycoprotein anchored to the outer layer of the plasma membrane through a glycosylphosphatidylinositol (GPI) anchor, which highly affects the structure and permeability of the yeast cell wall.
Abstract: The aim of the study was the identification, cloning and disruption of the GAS1 homologue of Pichia pastoris. Gas1p is a glycoprotein anchored to the outer layer of the plasma membrane through a glycosylphosphatidylinositol (GPI) anchor. Gas1p is a beta-1,3-glucanosyltransglycosylase (EC 2.4.1.-). This cross-linking enzyme highly affects the structure and permeability of the yeast cell wall. The gene coding for the GAS1 homologue of P. pastoris was cloned by PCR, and its functionality was proven in a Saccharomyces cerevisiae GAS1 null mutant. Based on the nucleotide sequence information of the P. pastoris GAS1 homologue, a disruption cassette was constructed for the knockout of the GAS1 in P. pastoris. The morphology of DeltaGAS1 P. pastoris was identical to that of S. cerevisiae GAS1 mutants. Finally, the impact of GAS1 disruption on secretion of three recombinant model proteins in P. pastoris, human trypsinogen, human serum albumin and Rhizopus oryzae lipase, was evaluated. While the disruption had no effect on the secretion of trypsinogen and albumin, the amount of lipase released from the cells was doubled.
46 citations
TL;DR: High-level extracellular production of Fusarium solani cutinase using a Pichia pastoris expression system was demonstrated for the first time and would be a promising alternative to many expression systems previously used for the large-scaleProduction of F. solanicutinase in Saccharomyces cerevisiae as well as Escherichia coli.
46 citations
TL;DR: This study indicated that the recombinant P. pastoris harboring 17β-HSD3 and G6PDH could be a promising candidate to produce TS in the pharmaceutical industry.
46 citations
Patent•
10 Dec 2002
TL;DR: In this paper, the polynucleotide coding sequence for simplified eukaryotic nitrate reductase (S-NaR1) was modified to 1.7.1.2 (formerly EC 1.6.2).
Abstract: The invention provides modification to the polynucleotide coding sequence for Pichia angusta NAD (P)H: nitrate reductase [YNaR1; GenBank accession number Z49110], which has Enzyme Commission number 1.7.1.2 (formerly EC 1.6.6.2), yielding the polynucleotide coding sequence for simplified eukaryotic nitrate reductase (S-NaR1). The invention also provides a method for recombinant expression of said polynucleotide code in the cells of the methylotrophic yeast Pichia pastoris to produce the polypeptide for S-NaR1, which binds the host-produced molybdenum-molybdopterin cofactor and intracellularly forms catalytically active, nitrate-reducing enzyme as small and stable multimeric proteins. The invention also provides a method for rapid and high-yielding purification of S-NaR1 by utilizing the hexa-histidine sequence at the carboxyl-terminus of said polypeptide for immobilized metal affinity chromatography.
45 citations
TL;DR: Endo-PGA1, cloned from the acidophilic fungus Bispora sp.
45 citations