Results 161 to 170 of about 10,440 (199)

Characterization of fermentation parameters, volatile compounds and microbial community structure of fermented grains in the upper and lower layers during strong-flavor Baijiu fermentation. [PDF]

Bioresour Bioprocess
Deng J, He CJ, Wei CH, Luo HB, Huang ZG.
europepmc   +1 more source

Whole Genome Sequencing of <i>Kodamaea ohmeri</i> SSK and Its Characterization for Degradation of Inhibitors from Lignocellulosic Biomass. [PDF]

Biology (Basel)
Yang YQ, Li X, Wang ZF, Deng YL, Wang ZZ, Fang XY, Zhang MD, Sun W, Zhao XQ, Liu ZQ, Zhang FL.   +10 more
europepmc   +1 more source

Production of Lactate by Metabolically Engineered <i>Scheffersomyces stipitis</i>. [PDF]

J Fungi (Basel)
Matanović A, Marđetko N, Slišković A, Didak B, Hanousek Čiča K, Žunar B, Štafa A, Šantek B, Svetec Miklenić M, Svetec IK.   +9 more
europepmc   +1 more source

Bifunctional alcohol/aldehyde dehydrogenase AdhE controls phospho-transferase system sugar utilization and virulence gene expression by interacting PtsH in Edwardsiella piscicida

Microbiological Research, 2022
The bifunctional alcohol/aldehyde dehydrogenase (AdhE), one of the key enzymes in the bacterial ethanol anaerobic fermentation pathway, is critical for appropriate expression of the genes for the utilization of carbon sources. Knowledge about its global roles in modulating gene expression and metabolomics remains limited. Edwardsiella bacteria includes
Qiaoqiao Mao, Jihao Jiang, Xiao Wu, Yue Ma, Yuanxing Zhang, Yanni Zhao, Yibei Zhang, Qiyao Wang   +7 more
openalex   +3 more sources

Polyol dehydrogenases: intermediate role in the bioconversion of rare sugars and alcohols

Applied Microbiology and Biotechnology, 2019
Polyol dehydrogenases (PDHs) play a pivotal role in the biotransformation between rare sugar and alcohol. Among these PDHs, mannitol 2-dehydrogenase (MDH, EC 1.1.1.67), galactitol 2-dehydrogenase (GDH, EC 1.1.1.16), ribitol 2-dehydrogenase (RDH, EC 1.1.1.56), xylitol 4-dehydrogenase (XDH, EC 1.1.1.14), and arabitol 2-dehydrogenase (ArDH, EC 1.1.1.12 ...
Fuzhi Lu, Wei Xu, Wenli Zhang, Cuie Guang, Wanmeng Mu   +4 more
openalex   +3 more sources

Membrane-bound dehydrogenases ofGluconobacter oxydans: Sensors for measuring sugars, alcohols, and polyoles

Bulletin of Experimental Biology and Medicine, 1998
The activity of membrane-bound dehydrogenases of immobilizedGluconobacter oxydans was used in ampero- and potentiometric biosensors for measuring glucose, ethanol, and glycerol. An amperometric biosensor was used for detection of glucose in human blood, glycerol in fermentation media, and ethanol vapors in the air.
А. Н. Решетилов, Marina V. Donova, Dmitry V. Dovbnya, P. V. Il’yasov, А. М. Боронин, T. Leasers, R. Green   +6 more
openalex   +2 more sources

Sugars protect native and apo yeast alcohol dehydrogenase against irreversible thermoinactivation

Enzyme and Microbial Technology, 2001
Abstract In the present study, irreversible thermoinactivation of holo- and apo-yeast alcohol dehydrogenase (YADH, EC 1.1.1.1) and protection by sugars (mannitol, sorbitol, sucrose and trehalose) were investigated at 50°C and pH 7.8. The apo-protein was obtained by removing the structural zinc with the catalytic zinc remaining on the enzyme.
Mehran Miroliaei, Mohsen Nemat‐Gorgani
openalex   +2 more sources

Behavior of Enzymes in the Presence of Additives Influence of Alcohóls, Polyols, and Sugars on Activity and Stability of Yeast Alcohol Dehydrogenase

Annals of the New York Academy of Sciences, 1988
L'effet stabilisant de differentes molecules est etudie sur l'alcool deshydrogenase de levure. Ces molecules sont des alcools avec des longueurs de chaines carbonees et/ou des nombres de groupements hydroxyles differents (monoalcool, dialcool, polyalcools avec un rapport OH/C egal a 1, c'est-a-dire des sucres).
Véronique Larreta‐Garde, ZU FENG XU, D. Thomas   +2 more
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Thermodynamic, kinetic, and operational stabilities of yeast alcohol dehydrogenase in sugar and compatible osmolyte solutions

Enzyme and Microbial Technology, 2008
Abstract Thermodynamic, kinetic, and operational stabilities of yeast alcohol dehydrogenase (YADH) were measured and compared in aqueous solutions containing various sugars (sucrose, glucose, and ribose) and compatible osmolytes (betaine and sarcosine).
Osato Miyawaki, MA Ge-li, Tomokazu Horie, Ayumi Hibi, Toru Ishikawa, Shoji Kimura   +5 more
openalex   +2 more sources