The methylotrophic yeasts Hansenula polymorpha and Trichosporon sp. revealed enhanced biodegradation capability of exogenously applied formaldehyde (Fd) upon biostimulation achieved by the presence of methanol, as compared to glucose. Upon growth on either of the above substrates, the strains proved to produce the activity of glutathione-dependent formaldehyde dehydrogenase-the enzyme known to control the biooxidative step of Fd detoxification. However, in the absence of methanol, the yeasts' tolerance to Fd was decreased, and the elevated sensitivity was especially pronounced for Trichosporon sp. Both strains responded to the methanol and/or Fd treatment by increasing their unsaturation index (UI) at xenobiotic levels below minimal inhibitory concentrations. This indicated that the UI changes effected from the de novo synthesis of (poly) unsaturated fatty acids carried out by viable cells. It is concluded that the yeast cell response to Fd intoxication involves stress reaction at the level of membranes. Fluidization of the lipid bilayer as promoted by methanol is suggested as a significant adaptive mechanism increasing the overall fitness enabling to cope with the formaldehyde xenobiotic via biodegradative pathway of C1-compound metabolism.
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http://dx.doi.org/10.1007/s00253-013-4796-y | DOI Listing |
J Biomol Struct Dyn
December 2024
Department of Bioinformatics, School of Life Sciences Pondicherry University, Puducherry, India.
Flavin adenine nucleotide (FAD)-dependent oxidoreductase enzyme Alcohol oxidase (AOX) facilitates the growth of methylotrophic yeast C. boidinii by catabolizing methanol, producing formaldehyde and hydrogen peroxide. Vacuolar Protease-A (PrA) from C.
View Article and Find Full Text PDFFolia Microbiol (Praha)
December 2024
Federal Research Center "Pushchino Scientific Center for Biological Research", Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Russian Federation.
Cells of the methylotrophic yeast Ogataea parapolymorpha have two genes encoding low-affinity phosphate transporters: PHO87, encoding the plasma membrane transporter, and PHO91, encoding a protein, which is homologous to the Saccharomyces cerevisiae vacuolar membrane transporter. Earlier, we reported that inactivation of PHO91 in O. parapolymorpha interferes with methanol utilization due to the lack of activity of methanol oxidase encoded by the MOX gene.
View Article and Find Full Text PDFBiotechnol Biofuels Bioprod
December 2024
Department of Chemical Engineering, Osaka Metropolitan University, 1-1 Gakuen-Cho, Naka-Ku, Sakai, Osaka, 599-8531, Japan.
Background: Currently, efficient technologies producing useful chemicals from alternative carbon resources, such as methanol, to replace petroleum are in demand. The methanol-utilizing yeast, Komagataella phaffii, is a promising microorganism to produce chemicals from methanol using environment-friendly microbial processes. In this study, to achieve efficient D-lactic acid production from methanol, we investigated a combination of D-lactate dehydrogenase (D-LDH) genes and promoters in K.
View Article and Find Full Text PDFSci Adv
December 2024
State Key Laboratory of Materials-Oriented Chemical Engineering, College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing 211800, China.
Methanol, as a non-edible feedstock, offers a promising sustainable alternative to sugar-based substrates in biochemical production. Despite progress in engineering methanol assimilation in nonmethylotrophs, the full transformation into methanol-dependent synthetic methylotrophs remains a formidable challenge. Here, moving beyond the conventional rational design principle, we engineered a synthetic methylotrophic through genome rearrangement and adaptive laboratory evolution.
View Article and Find Full Text PDFBiosci Biotechnol Biochem
December 2024
Technology Innovation Strategy and Intelligence, Daiichi Sankyo Co., Ltd., Chiyoda, Gunma, Japan.
Methylotrophic yeast is a useful host for producing heterologous proteins using the unique and strong alcohol oxidase 1 (AOX1) promoter, which is induced by methanol and repressed by various carbon sources. However, methanol is preferably avoided in industrial-scale fermentation given its toxicity, flammability, and explosiveness. To develop a protein production system under reduced methanol supply conditions, we attempted to characterize the AOX1 promoter induction activity by comparing derepression conditions with methanol induction conditions.
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