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: HirJM79, a Sec-dependent bacteriocin produced by Enterococcus hirae DCH5, was cloned and produced in Lactococcus lactis, Lactobacillus sakei,Enterococcus faecium, Enterococus faecalis, and Pichia pastoris, although the antimicrobial activities of most transformants were lower than that predicted from their production of HirJM79.
Abstract: Hiracin JM79 (HirJM79), a Sec-dependent bacteriocin produced by Enterococcus hirae DCH5, was cloned and produced in Lactococcus lactis, Lactobacillus sakei, Enterococcus faecium, Enterococcus faecalis, and Pichia pastoris. For heterologous production of HirJM79 in lactic acid bacteria (LAB), the HirJM79 structural gene (hirJM79), with or without the HirJM79 immunity gene (hiriJM79), was cloned into the plasmid pMG36c under the control of the constitutive promoter P32 and into the plasmid pNZ8048 under the control of the inducible PNisA promoter. For the production of HirJM79 in P. pastoris, the gene encoding the mature HirJM79 protein was cloned into the pPICZαA expression vector. The recombinant plasmids permitted the production of biologically active HirJM79 in the supernatants of L. lactis IL1403, L. lactis NZ9000, L. sakei Lb790, E. faecalis JH2-2, and P. pastoris X-33, the coproduction of HirJM79 and nisin A in L. lactis DPC5598, and the coproduction of HirJM79 and enterocin P in E. faecium L50/14-2. All recombinant LAB produced larger quantities of HirJM79 than E. hirae DCH5, although the antimicrobial activities of most transformants were lower than that predicted from their production of HirJM79. The synthesis, processing, and secretion of HirJM79 proceed efficiently in recombinant LAB strains and P. pastoris.
53 citations
TL;DR: The human mu-opioid receptor (HuMOR) was fused in its N-terminus end to the green fluorescent protein (GFP) or/and to the c-myc and six histidines tags in its C-terminal end, and expressed in the methylotrophic yeast Pichia pastoris as discussed by the authors.
53 citations
TL;DR: This study characterised, for the first time, the effects of five commonly-used antifoaming agents on the total amount of recombinant green fluorescent protein secreted from shake-flask cultures of this industrially-relevant yeast.
Abstract: Pichia pastoris is a widely-used host for recombinant protein production. Initial screening for both suitable clones and optimum culture conditions is typically carried out in multi-well plates. This is followed by up-scaling either to shake-flasks or continuously stirred tank bioreactors. A particular problem in these formats is foaming, which is commonly prevented by the addition of chemical antifoaming agents. Intriguingly, antifoams are often added without prior consideration of their effect on the yeast cells, the protein product or the influence on downstream processes such as protein purification. In this study we characterised, for the first time, the effects of five commonly-used antifoaming agents on the total amount of recombinant green fluorescent protein (GFP) secreted from shake-flask cultures of this industrially-relevant yeast.
53 citations
01 Jan 1999
TL;DR: A better understanding of P. pastoris proteases and, in particular, the identification of those responsible for the degradation of some foreign proteins would aid in the development of strategies to eliminate or circumvent their effects.
Abstract: The pichia pastoris expression system has gained acceptance as an important host organism for the production of foreign proteins. This chapter provides a basic understanding of the P. pastoris expression system and deals with various questions related to it, essentially describing how this system works. The chapter explains the proteins that are most likely to work well in the system, the problems to anticipate while using it, and potential solutions. The chapter discusses the success of the P. pastoris system and exclaims that opportunities still exist to increase the range of proteins that can be expressed in the system. The discussion concludes with the fact that studies are required to address problems associated with the secretion of mammalian proteins from P. pastoris . There are certain questions that need to be resolved, which require further study of this expression system. Thus, a better understanding of P. pastoris proteases and, in particular, the identification of those responsible for the degradation of some foreign proteins would aid in the development of strategies to eliminate or circumvent their effects.
52 citations
TL;DR: This study biochemically characterized the plasma membrane of the methylotrophic yeast Pichia pastoris with emphasis on the lipids which form the matrix of this compartment, and found it to be enriched in plasma membrane fractions, although markedly lower than in Saccharomyces cerevisiae.
52 citations