A major problem in fermenting xylose in lignocellulosic substrates is the presence of glucose and mannose which inhibit xylose utilization. Previous studies showed that catabolite repression in some yeasts is associated with hexokinases and that deletion of one of these gene(s) could result in derepressed mutant strain(s). In this study, the hxk1 encoding hexokinase 1 in Scheffersomyces stipitis was disrupted. The ∆hxk1 SS6 strain retained the ability to utilize the main hexoses and pentoses commonly found in lignocellulosic hydrolysates as efficiently as the wild-type (WT) strain. SS6 also fermented the dominant sugars to ethanol; however, on xylose, the ∆hxk1 strain produced more xylitol and less ethanol than the WT. On mixed sugars, as expected the WT utilized glucose ahead of xylose and xylose utilization did not commence until all the glucose was consumed. In contrast, the ∆hxk1 mutant showed derepression in that it started to utilize xylose even when considerable glucose (about 1.72%, w/v) remained in the medium. Similarly, mannose did not repress xylose utilization by the ∆hxk1 mutant and xylose and mannose were simultaneously utilized. The results are of interest in efforts to engineer yeast strains capable of efficiently utilizing glucose and xylose simultaneously for lignocellulosic biomass conversion.
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http://dx.doi.org/10.1007/s10295-015-1614-9 | DOI Listing |
Synth Syst Biotechnol
June 2025
Division of Biotechnology, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, 457 Zhongshan Road, Dalian, 116023, PR China.
Lignocellulose bio-refinery via microbial cell factories for chemical production represents a renewable and sustainable route in response to resource starvation and environmental concerns. However, the challenges associated with the co-utilization of xylose and glucose often hinders the efficiency of lignocellulose bioconversion. Here, we engineered yeast to effectively produce free fatty acids from lignocellulose.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
College of Pharmaceutical Science, Dali University, Dali 671000, China; International Joint Laboratory for the Development and Utilization of Traditional Chinese Medicine Resources in Yunnan Province, Baoshan 678300, Dali 671000, China. Electronic address:
Ficus carica (F. carica) is a well-known medicinal and edible plant with high nutritive values. Polysaccharides are the primary and important bioactive components in F.
View Article and Find Full Text PDFAnal Methods
January 2025
Key Laboratory of Xin'an Medicine of the Ministry of Education, College of Chinese Medicine, School of Pharmacy, Anhui University of Chinese Medicine, Hefei, 230038, P. R. China.
4-Amidogen-1,8-naphthalimide (ANA), a novel pre-column derivatization reagent, has been successfully synthesized and utilized for the highly sensitive analysis of monosaccharides. ANA reacts with the reducing carbonyl groups of saccharides, facilitating monosaccharide detection. The resulting monosaccharide derivatives were meticulously investigated using High-Performance Liquid Chromatography (HPLC) coupled with ultraviolet (UV) spectroscopy.
View Article and Find Full Text PDFPrep Biochem Biotechnol
January 2025
College of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou, Zhejiang Province, People's Republic of China.
Myo-inositol is an active sugar alcohol which has important physiological functions. In this study, an engineered strain that could simultaneously utilize glucose and xylose to produce myo-inositol was constructed, and its fermentation performance was determined. Firstly, the gene was deleted to make BL21 capable of utilizing glucose and xylose simultaneously as mixed carbon source.
View Article and Find Full Text PDFJ Biol Chem
January 2025
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto, 606-8502, Japan. Electronic address:
Many patients with diabetes use self-measurement devices for blood glucose to understand their blood glucose levels. Most of these devices utilize FAD-dependent glucose dehydrogenase (FAD-GDH) to determine blood glucose levels. For this purpose, FAD-GDHs specifically oxidizing glucose among the sugars present in blood is required.
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