Production of xylitol by expressing xylitol dehydrogenase and alcohol dehydrogenase from Gluconobacter thailandicus and co-biotransformation of whole cells

2018 ◽  
Vol 257 ◽  
pp. 223-228 ◽  
Author(s):  
Huanhuan Zhang ◽  
Junhua Yun ◽  
H. Zabed ◽  
Miaomiao Yang ◽  
Guoyan Zhang ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Xylitol Dehydrogenase ◽  
Whole Cells

Pyruvate Decarboxylase Catalyzes Decarboxylation of Branched-Chain 2-Oxo Acids but Is Not Essential for Fusel Alcohol Production by Saccharomyces cerevisiae

1998 ◽  
Vol 64 (4) ◽  
pp. 1303-1307 ◽  
Author(s):  
Eelko G. ter Schure ◽  
Marcel T. Flikweert ◽  
Johannes P. van Dijken ◽  
Jack T. Pronk ◽  
C. Theo Verrips
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Alcohol Dehydrogenase ◽  
Pyruvate Decarboxylase ◽  
Wild Type ◽  
Alcohol Production ◽  
Whole Cells ◽  
Fusel Alcohols ◽  
Cell Extracts ◽  
Fusel Alcohol ◽  
Branched Chain

ABSTRACT The fusel alcohols 3-methyl-1-butanol, 2-methyl-1-butanol, and 2-methyl-propanol are important flavor compounds in yeast-derived food products and beverages. The formation of these compounds from branched-chain amino acids is generally assumed to occur via the Ehrlich pathway, which involves the concerted action of a branched-chain transaminase, a decarboxylase, and an alcohol dehydrogenase. Partially purified preparations of pyruvate decarboxylase (EC 4.1.1.1 ) have been reported to catalyze the decarboxylation of the branched-chain 2-oxo acids formed upon transamination of leucine, isoleucine, and valine. Indeed, in a coupled enzymatic assay with horse liver alcohol dehydrogenase, cell extracts of a wild-type Saccharomyces cerevisiae strain exhibited significant decarboxylation rates with these branched-chain 2-oxo acids. Decarboxylation of branched-chain 2-oxo acids was not detectable in cell extracts of an isogenic strain in which all threePDC genes had been disrupted. Experiments with cell extracts from S. cerevisiae mutants expressing a singlePDC gene demonstrated that both PDC1- andPDC5-encoded isoenzymes can decarboxylate branched-chain 2-oxo acids. To investigate whether pyruvate decarboxylase is essential for fusel alcohol production by whole cells, wild-type S. cerevisiae and an isogenic pyruvate decarboxylase-negative strain were grown on ethanol with a mixture of leucine, isoleucine, and valine as the nitrogen source. Surprisingly, the three corresponding fusel alcohols were produced in both strains. This result proves that decarboxylation of branched-chain 2-oxo acids via pyruvate decarboxylase is not an essential step in fusel alcohol production.

scholarly journals The aromatic alcohol dehydrogenases in Pseudomonas putida N.C.I.B. 9869 grown on 3,5-xylenol and p-cresol

1978 ◽  
Vol 175 (2) ◽  
pp. 659-667 ◽  
Author(s):  
M J Keat ◽  
D J Hopper
Keyword(s):  
Alcohol Dehydrogenase ◽  
Pseudomonas Putida ◽  
The Other ◽  
Alcohol Dehydrogenases ◽  
Whole Cells ◽  
Aromatic Alcohol ◽  
Aromatic Alcohols ◽  
Hydroxybenzyl Alcohol

Whole cells of Pseudomonas putida N.C.I.B 9869, when grown on either 3,5-xylenol or p-cresol, oxidized both m- and p-hydroxybenzyl alcohols. Two distinct NAD+-dependent m-hydroxybenzyl alcohol dehydrogenases were purified from cells grown on 3,5-xylenol. Each is active with a range of aromatic alcohols, including both m- and p-hydroxybenzyl alcohol, but differ in their relative rates with the various substrates. An NAD+-dependent alcohol dehydrogenase was also partially purified from p-cresol grown cells. This too was active with m- and p-hydroxybenzyl alcohol and other aromatic alcohols, but was not identical with either of the other two dehydrogenases. All three enzymes were unstable, but were stabilized by dithiothreitol and all were inhibited with p-chloromercuribenzoate. All were specific for NAD+ and each was shown to catalyse conversion of alcohol into aldehyde.

An effective hybrid strategy for converting rice straw to furoic acid by tandem catalysis via Sn-sepiolite combined with recombinant E. coli whole cells harboring horse liver alcohol dehydrogenase

2019 ◽  
Vol 21 (21) ◽  
pp. 5914-5923 ◽  
Author(s):  
Bo Peng ◽  
Cui-Luan Ma ◽  
Peng-Qi Zhang ◽  
Chang-Qing Wu ◽  
Zi-Wei Wang ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Rice Straw ◽  
Tandem Catalysis ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Hybrid Strategy ◽  
Furoic Acid ◽  
Whole Cells ◽  
E Coli ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver

The upgrading of biomass-derived furfural into high-value bio-based chemicals has attracted interest.

Alcohol dehydrogenase activity in Rhodotorula glutinis

1973 ◽  
Vol 19 (3) ◽  
pp. 353-358 ◽  
Author(s):  
Casimir J. Woscinski ◽  
Dan O. McClary
Keyword(s):  
Alcohol Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Rhodotorula Glutinis ◽  
Cinnamyl Alcohol Dehydrogenase ◽  
Cinnamyl Alcohol ◽  
Glucose Medium ◽  
Whole Cells ◽  
Alcohol Dehydrogenase Activity ◽  
Ethanol Medium ◽  
Significant Difference

Whole-cell extracts of Rhodotorula glutinis grown on yeast extract – glucose medium contained minute quantities of NAD-dependent alcohol dehydrogenase and cinnamyl alcohol dehydrogenase. Significantly greater quantities of these enzymes, as well as an NADP-dependent alcohol dehydrogenase were contained by cells grown on the same medium with ethanol substituted for glucose as the growth substrate. Although the [Formula: see text] on ethanol of whole cells grown in ethanol medium was more than triple that of cells grown in glucose medium, there was no significant difference in the [Formula: see text] on glucose of whole cells grown in glucose or in ethanol medium. Thermal inactivation studies revealed that the NADP-dependent alcohol dehydrogenase was relatively heat-stable as compared with the NAD-dependent alcohol dehydrogenase. Gel column electrophoresis revealed three active bands of alcohol dehydrogenase activity which were identified as NAD-dependent alcohol dehydrogenase, NADP-dependent alcohol dehydrogenase, and cinnamyl alcohol dehydrogenase. The NAD- and NADP-dependent enzymes, particularly the latter, were active on higher alcohols but not on methanol.

Efficient biosynthesis of enantiopure tolvaptan by utilizing alcohol dehydrogenase-catalyzed enantioselective reduction

2018 ◽  
Vol 20 (6) ◽  
pp. 1224-1227 ◽  
Author(s):  
Hong-Lei Zhang ◽  
Chao Zhang ◽  
Meng-Nan Han ◽  
Chao-Hong Pei ◽  
Zhi-Dong Xu ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Alcohol Dehydrogenase ◽  
Soybean Oil ◽  
Efficient Method ◽  
Formate Dehydrogenase ◽  
Whole Cells ◽  
Enantioselective Reduction

Using whole cells of Escherichia coli co-expressing alcohol dehydrogenase (PsADH) and formate dehydrogenase (CpFDH) in a biphasic aqueous–soybean oil system is shown to be an efficient method for the biosynthesis of enantiopure tolvaptan.

Low temperature x-ray microanalysis of frozen-hydrated tobacco leaves

1984 ◽  
Vol 42 ◽  
pp. 284-285
Author(s):  
S. Edith Taylor ◽  
Patrick Echlin ◽  
May McKoon ◽  
Thomas L. Hayes
Keyword(s):  
Low Temperature ◽  
Lemna Minor ◽  
Root Tips ◽  
Tobacco Leaves ◽  
X Ray ◽  
Whole Cells ◽  
Carbon Coated ◽  
The Right ◽  
Beam Currents ◽  
The University

Low temperature x-ray microanalysis (LTXM) of solid biological materials has been documented for Lemna minor L. root tips. This discussion will be limited to a demonstration of LTXM for measuring relative elemental distributions of P,S,Cl and K species within whole cells of tobacco leaves.Mature Wisconsin-38 tobacco was grown in the greenhouse at the University of California, Berkeley and picked daily from the mid-stalk position (leaf #9). The tissue was excised from the right of the mid rib and rapidly frozen in liquid nitrogen slush. It was then placed into an Amray biochamber and maintained at 103K. Fracture faces of the tissue were prepared and carbon-coated in the biochamber. The prepared sample was transferred from the biochamber to the Amray 1000A SEM equipped with a cold stage to maintain low temperatures at 103K. Analyses were performed using a tungsten source with accelerating voltages of 17.5 to 20 KV and beam currents from 1-2nA.

Discovery of intracellular 2,8 dihydroxyadenine crystals in bovine lymphatic and hepatic cells

1987 ◽  
Vol 45 ◽  
pp. 906-907
Author(s):  
W. E. Rigsby ◽  
D. M. Hinton ◽  
V. J. Hurst ◽  
P. C. McCaskey
Keyword(s):  
Polarized Light ◽  
Paraffin Sections ◽  
Tissue Samples ◽  
Whole Cells ◽  
Tissue Sections ◽  
Hepatic Cells ◽  
Slaughter House ◽  
Mammalian Tissues ◽  
Carbon Coated ◽  
Cellular Components

Crystalline intracellular inclusions are rarely seen in mammalian tissues and are often difficult to positively identify. Lymph node and liver tissue samples were obtained from two cows which had been rejected at the slaughter house due to the abnormal appearance of these organs in the animals. The samples were fixed in formaldehyde and some of the fixed material was embedded in paraffin. Examination of the paraffin sections with polarized light microscopy revealed the presence of numerous crystals in both hepatic and lymph tissue sections. Tissue sections were then deparaffinized in xylene, mounted, carbon coated, and examined in a Phillips 505T SEM equipped with a Tracor Northern X-ray Energy Dispersive Spectroscopy (EDS) system. Crystals were obscured by cellular components and membranes so that EDS spectra were only obtainable from whole cells. Tissue samples which had been fixed but not paraffin-embedded were dehydrated, embedded in Spurrs plastic, and sectioned.

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