The induction of xylose reductase and xylitol dehydrogenase activities on mixed sugars was investigated in the yeasts Pachysolen tannophilus and Pichia stipitis. Enzyme activities induced on d-xylose served as the controls. In both yeasts, d-glucose, d-mannose, and 2-deoxyglucose inhibited enzyme induction by d-xylose to various degrees. Cellobiose, l-arabinose, and d-galactose were not inhibitory. In liquid batch culture, P. tannophilus utilized d-glucose and d-mannose rapidly and preferentially over d-xylose, while d-galactose consumption was poor and lagged behind that of the pentose sugar. In P. stipitis, all three hexoses were used preferentially over d-xylose. The results showed that the repressibility of xylose reductase and xylitol dehydrogenase may limit the potential of yeast fermentation of pentose sugars in hydrolysates of lignocellulosic substrates.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC202395 | PMC |
| http://dx.doi.org/10.1128/aem.54.1.50-54.1988 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Deciphering the core shunt mechanism in Arabidopsis cuticular wax biosynthesis and its role in plant environmental adaptation.
Nat Plants
January 2025
State Key Laboratory of Biocatalysis and Enzyme Engineering, School of Life Sciences, Hubei University, Wuhan, China.
Plant cuticular waxes serve as highly responsive adaptations to variable environments. Aliphatic waxes consist of very-long-chain (VLC) compounds produced from 1-alcohol- or alkane-forming pathways. The existing variation in 1-alcohols and alkanes across Arabidopsis accessions revealed that 1-alcohol amounts are negatively correlated with aridity factors, whereas alkanes display the opposite behaviour.
View Article and Find Full Text PDFMultienzyme cascade for synthesis of hydroxytyrosol via engineered Escherichia coli.
Sci Rep
January 2025
Dabie Mountain Laboratory, College of Tea and Food Science, Xinyang Normal University, Xinyang, 464000, Henan, China.
Hydroxytyrosol, a fine chemical, is widely utilized in food and pharmaceutical industries. In this study, we constructed a pathway to produce hydroxytyrosol by co-expressing tyrosin-phenol lyase (TPL), L-amino acid dehydrogenase (aadL), α-keto acid decarboxylase (KAD), aldehyde reductase (yahK) and glucose dehydrogenase (gdh). We changed combinations between plasmids with different copy numbers and target genes, resulting in 84% increase in hydroxytyrosol production.
View Article and Find Full Text PDFIdentification and validation of Novel Estrogen Biosynthesis Biomarkers in Sinonasal Inverted Papilloma.
Int J Med Sci
January 2025
Department of Otolaryngology, Head and Neck Surgery, Kaohsiung Veterans General Hospital, Kaohsiung 813, Taiwan.
Article Synopsis
- Sinonasal inverted papilloma (SNIP) has a high recurrence rate and the potential to become malignant, but its specific metabolic pathways and biomarkers are not fully understood.
- RNA sequencing identified significant gene alterations related to the estrogen biosynthesis pathway and highlighted five key biomarkers (AKR1B10, CYP1B1, CYP2C19, CYP3A5, and HSD17B13) that were correlated with SNIP pathogenesis.
- Functional analysis indicated that these biomarkers are involved in epithelial cell proliferation and EGFR signaling regulation, suggesting their potential as diagnostic and therapeutic targets for managing SNIP.
Synergistic effect of alkane and membrane lipid alteration in Synechococcus elongatus PCC 7942 under salt and light stresses.
J Plant Res
December 2024
Graduate School of Science and Technology, Shizuoka University, Suruga-ku, Shizuoka, 422-8529, Japan.
Salinity and light markedly influence cyanobacterial viability. High salinity disrupts the osmotic balance, while excess light energy affects redox potential in the cells. Regulating the ratio of saturated and unsaturated alka(e)ne and fatty acids in cyanobacteria is thought to have crucial roles in coping with these stresses by regulating membrane fluidity.
View Article and Find Full Text PDFALDH Enzymes and Hematological Diseases: A Scoping Review of Literature.
Discov Med
December 2024
Department of Biological Hematology, Tours University Hospital, 37000 Tours, France.
Aldehyde dehydrogenases (ALDHs) constitute a group of enzymes that catalyze the oxidation of aldehydes to carboxylic acids. The human ALDH superfamily, including 19 different isoenzymes (ALDH1A1, ALDH1A2, ALDH1A3, AHDH1B1, ALDH1L1, ALDH1L2, ALDH2, ALDH3A1, ALDH3A2, ALDH3B1, ALDH3B2, ALDH4A1, ALDH5A1, ALDH6A1, ALDH7A1, ALDH8A1, ALDH9A1, ALDHA16A1, ALDH18A1), displays different key physiological and toxicological functions, with specific tissue expression and substrate specificity. Several studies have established that ALDH are interesting markers for the identification and quantification of human hematopoietic stem cells and cancer stem cells, notably leukemic stem cells.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!