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1.
《Bioscience, biotechnology, and biochemistry》2013,77(2):298-303
A benzyl alcohol oxidase (BAO) was purified to homogeneity from Botrytis cinerea. The enzyme was found to have a molecular mass of 214 kD with a trimeric structure, and optimal pH and temperature of 5.0 and 30°C, respectively. The enzyme activity was not sensitive to metal ions or to metal ion chelators, while thiol blocking reagents strongly inhibited BAO activity. Sulfur dioxide irreversibly inhibited the enzyme activity and the inhibitory effect of ethanol was weak and reversible. Benzyl alcohol was the most effective alcohol substrate for BAO. Para or meta monosubstituted benzyl alcohol with methyl or methoxy groups were good substrates. BAO also oxidized cinnamyl alcohol, furfuryl alcohol, and some terpenic alcohols· with an alkenyl group near the reactive carbinol. Secondary alcohol, methanol and phenol were not substrates. Product inhibition studies suggested that benzaldehyde and benzyl alcohol were bound at different places to the active site. O2 was the only electron acceptor identified and Botrytis cinerea benzyl alcohol oxidase was classified .as EC 1.1.3.7 according to stoichiometrical studies. We discuss the metabolic role of BAO in the Botrytis cinerea-grape host-parasite relationship. 相似文献
2.
During the study of aerobic dissimilation of galactose by yeasts, polyhydric products were isolated in crystalline form from the fermented broths and identified. Yeast species may be divided into two groups on basis of sugar alcohol production: type I yeasts form the same end products from galactose as from glucose; type II yeasts produce dulcitol from galactose with or without other sugar alcohols but they produce no dulcitol from glucose. Isolation of dulcitol from microorganism has not been previously described. 相似文献
3.
Arjan Siebum Arjan van Wijk Rob Schoevaart Tom Kieboom 《Journal of Molecular Catalysis .B, Enzymatic》2006,41(3-4):141-145
The utility of both galactose oxidase and alcohol oxidase for alcohol-to-aldehyde oxidation has been investigated, from a synthetic point of view. The speed of reaction and degree of conversion has been measured for 29 different primary alcohols. The two oxidative enzymes show complementary synthetic use, i.e. galactose oxidase for galactose-derived polyols and alcohol oxidase for aliphatic mono- and diols. Alcohol oxidase has been successfully used in combination with the aldolase DERA in a two-step, one-pot reaction cascade. 相似文献
4.
J. J. van der Waarde R. Kok D. B. Janssen 《Applied microbiology and biotechnology》1994,42(1):158-166
The biodegradation of chloroallyl alcohols by pure and mixed bacterial cultures was investigated. Only 2-chloroallyl alcohol and cis- and trans-3-chloroallyl alcohol served as growth substrate for pure cultures. The other chloroallyl alcohols could be cometabolically degraded during growth on 2-chloroallyl alcohol. Cometabolic degradation of trichloroallyl alcohol, which was the most recalcitrant congener, by a Pseudomonas strain isolated on 2-chloroallyl alcohol resulted in 60% dechlorination. Efficient degradation of a mixture of chloroallyl alcohols in continuous culture could only be achieved in the presence of a satellite population. The mixed culture degraded 99% of the total chloroallyl alcohols added with 71% chloride release. The culture contained strains with a new catabolic potential. The results indicate the importance of mixed cultures and genetic adaptation for efficient chloroallyl alcohol removal. 相似文献
5.
The influence of water-miscible alcohols (methanol, 1-propanol, 2-propanol, and t-butyl alcohol) on the isomerization of glucose to fructose and mannose was investigated under subcritical aqueous conditions (180–200 °C). Primary and secondary alcohols promoted the conversion and isomerization of glucose to afford fructose and mannose with high and low selectivity, respectively. On the other hand, the decomposition (side-reaction) of glucose was suppressed in the presence of the primary and secondary alcohols compared with that in subcritical water. The yield of fructose increased with increasing concentration of the primary and secondary alcohols, and the species of the primary and secondary alcohols tested had little effect on the isomerization behavior of glucose. In contrast, the isomerization of glucose was suppressed in subcritical aqueous t-butyl alcohol. Both the conversion of glucose and the yield of fructose decreased with increasing concentration of t-butyl alcohol. In addition, mannose was not detected in reactions using subcritical aqueous t-butyl alcohol. 相似文献
6.
Effect of glucose and long-chain fatty acids on synthesis of long-chain alcohols by Candida albicans
Candida albicans, grown aerobically in glucose-containing media, produced C14, C16 and C18 saturated long-chain alcohols only after the end of exponential growth. Contents of C14 alcohols were always lowest, and C16 and C18 alcohol contents about equal. Contents of all three classes of alcohol increased as the concentration of glucose in aerobic cultures harvested after 168 h incubation was raised from 1.0 to 30.0% (w/v). However, in 168 h anaerobic cultures, greatest long-chain alcohol contents in organisms were obtained using media containing 10% (w/v) glucose. Substituting glucose (10%, w/v) with the same concentration of galactose in aerobic cultures greatly decreased contents of long-chain alcohols, while inclusion of 10% (w/v) glycerol virtually abolished their synthesis. Supplementing anaerobic cultures with odd-chain fatty acids induced synthesis of odd-chain alcohols. Maximum conversion of fatty acid to the corresponding long-chain alcohol was observed with heptadecanoic acid. The effect of glucose on production of heptadecanol from exogenously provided heptadecanoic acid was similar to that observed on synthesis of the three major even-chain alcohols in media lacking a fatty-acid supplement. Cell-free extracts of organisms catalysed in vitro conversion of palmitoyl-CoA to 1-hexadecanol. 相似文献
7.
V. S. O'Leary R. Green B. C. Sullivan V. H. Holsinger 《Biotechnology and bioengineering》1977,19(7):1019-1035
Ethanol production by Kluyveromyces fragilis and Saccharomyces cerevisiae was studied using cottage cheese whey in which 80 to 90% of the lactose present had been prehydrolyzed to glucose and galactose. Complete fermentation of the sugar by K. fragilis required 120 hr at 30°C in lactase-hydrolyzed whey compared to 72 hr in nonhydrolyzed whey. This effect was due to a diauxic fermentation pattern in lactase-hydrolyzed whey with glucose being fermented before galactose. Ethanol yields of about 2% were obtained in both types of whey when K. fragilis was the organism used for fermentation. Saccharomyces cerevisiae produced alcohol from glucose more rapidly than K. fragilis, but galactose was fermented only when S. cerevisiae was pregrown on galactose. Slightly lower alcohol yields were obtained with S. cerevisiae, owing to the presence of some lactose in the whey which was not fermented by this organism. Although prehydrolysis of lactose in whey and whey fractions is advantageous in that microbial species unable to ferment lactose may be utilized, diauxie and galactose utilization problems must be considered. 相似文献
8.
Rhizomorph Formation in Fungi 总被引:1,自引:0,他引:1
The effect on growth and rhizomorph formation of 12 alcohols (methanol, ethanol, 1-propanol, 2-propanol, 1-butanol, 2-butanol, iso-butyl alcohol, tert-butyl alcohol, 1-pentanol, iso-amyl alcohol, ethylene glycol and glycerol) at different concentrations has been examined for 2 isolates of Armillaria mellea (Vahl ex Fr.) Quél. and 1 of Clitocybe geotropa (Bull. ex Fr.) Quél. The fungi were cultivated for 28 days on a synthetic, liquid glucose medium with the alcohols as supplement. The following alcohols strongly stimulated growth and rhizomorph formation: ethanol, 1-propanol and 1-butanol. A great variation was demonstrated between the isolates in relation to rhizomorph production, morphology, and ability to be stimulated by different alcohols. 相似文献
9.
V. S. O'leary C. Sutton M. Bencivengo B. Sullivan V. H. Holsinger 《Biotechnology and bioengineering》1977,19(11):1689-1702
Alcohol yields of 6.5% were obtained with Saccharomyces cerevisiae in lactasehydrolyzed acid whey permeate containing 30–35% total solids. Maximum alcohol yields obtained with Kluyveromyces fragilis were 4.5% in lactase-hydrolyzed acid whey permeate at a solids concentration of 20% and 3.7% in normal permeate at a solids concentration of 10%. Saccharomyces cerevisiae efficiently converted the glucose present in lactase-hydrolyzed whey permeates containing 5–30% total solids (2–13% glucose) to alcohol. However, the galactose, which comprised about half the available carbohydrate in lactase-hydrolyzed whey, was not utilized by S. cerevisiae, so that even though alcohol yields were higher when this organism was used, the process was wasteful in that a substantial proportion of the substrate was not fermented. For the process to become commercially feasible, an efficient means of rapidly converting both the galactose and glucose to alcohol must be found. 相似文献
10.
Peng X Taki H Komukai S Sekine M Kanoh K Kasai H Choi SK Omata S Tanikawa S Harayama S Misawa N 《Applied microbiology and biotechnology》2006,71(6):824-832
Four genes were isolated and characterized for alcohol dehydrogenases (ADHs) catalyzing the oxidation of aromatic alcohols such as benzyl alcohol to their corresponding aldehydes, one from o-xylene-degrading Rhodococcus
opacus TKN14 and the other three from n-alkane-degrading Rhodococcus
erythropolis PR4. Various aromatic alcohols were bioconverted to their corresponding carboxylic acids using Escherichia
coli cells expressing each of the four ADH genes together with an aromatic aldehyde dehydrogenase gene (phnN) from Sphingomonas sp. strain 14DN61. The ADH gene (designated adhA) from strain TKN14 had the ability to biotransform a wide variety of aromatic alcohols, i.e., 2-hydroxymethyl-6-methylnaphthalene, 2-hydroxymethylnaphthalene, xylene-α,α’-diol, 3-chlorobenzyl alcohol, and vanillyl alcohol, in addition to benzyl alcohol with or without a hydroxyl, methyl, or methoxy substitution. In contrast, the three ADH genes of strain PR4 (designated adhA, adhB, and adhC) exhibited lower ability to degrade these alcohols: these genes stimulated the conversion of the alcohol substrates by only threefold or less of the control value. One exception was the conversion of 3-methoxybenzyl alcohol, which was stimulated sevenfold by adhB. A phylogenetic analysis of the amino acid sequences of these four enzymes indicated that they differed from other Zn-dependent ADHs.The first two authors contributed equally to this work 相似文献
11.
The amounts of isobutyl and isoamyl alcohol which are the main constituents of fusel oil are determined fractionally. Isobutyl and isoamyl alcohol give different colors by treatment with p-dimethylaminobenzaldehyde in sulfuric acid. Using this color difference the amount of each of these alcohols in fusel oil is determined colorimetrically. These alcohols arise during alcoholic fermentation and are concentrated in the distillate by distillation, and affect the flavor of distilled spirits, such as brandy and whisky, i.e., butyl alcohol is buttery and amyl alcohol is aromatic. So determination of the amounts of these alcohols fractionally in these spirits furnishes a useful criterion for evaluating the character of these spirits. 相似文献
12.
Kiyoshi Yoshizawa Toshiro Furukawa Makoto Tadenuma Masakazu Yamada 《Bioscience, biotechnology, and biochemistry》2013,77(4):326-332
We have found that some straight-chained α-amino acids are converted by yeast to the alcohols with correspondingly longer carbon chains in the alcoholic fermentation contrary to F. Ehrlich’s scheme, i.e., isobutyl alcohol from alanine and active amyl alcohol from α-amino-n-butyric acid or threonine.In this report, we confirmed this fact in the alcoholic fermentation of many aliphatic amino acids by 2 yeast strains using gas chromatography. Moreover, n-propyl alcohol was proved to come from α-amino-n-butyric acid or threonine. Small quantities of n-propyl, isobutyl, active amyl and isoamyl alcohols were found in all the fermented solutions. There was some difference in the composition of higher alcohols of the alcoholic solutions fermented by different yeasts. 相似文献
13.
- 1. 1. Anesthetic alcohols (pentanol, hexanol and heptanol) were found to increase the fluidity of red cell membrane lipids as monitored by the fluorescence depolarization of diphenylhexatriene. The relative potency of the alcohols was found to be parallel to their relative membrane/water partition coefficients.
- 2. 2. Hexanol had biphasic effect on erythritol uptake by simple diffusion by red cells. At concentrations less than 9 mM, hexanol had no significant effect. At concentrations greater than 9 mM, there was an approximately linear increase in erythritol permeability with increasing alcohol concentration.
- 3. 3. The facilitated transport of uridine was markedly inhibited by hexanol. Hexanol at 6 mM produced a 65% inhibition of uridine (4 mM) uptake. Hexanol decreased both the apparent Km and V values for the equilibrium exchange of uridine.
- 4. 4. The facilitated transport of galactose was only slightly inhibited by hexanol.
- 5. 5. Hexanol was without effect on the passive and active fluxes of Na+ and K+ in red cells with altered cation contents. Cells that were slightly depleted of K+ and cells that were highly K+-depleted were both insensitive to hexanol.
Keywords: Anesthetic alcohol; Transport; (Human erythrocyte membrane) 相似文献
14.
Summary The alcohol-oxidase-mediated oxidation of hexanol to hexanal was conducted by whole cells of Pichia pastoris in a biphasic reaction medium consisting of 3% water and 97% (v/v) water-saturated hexane. At substrate levels of ca. 10 g/l, hexanal was produced at a rate of 0.2 g/g cell dry wt. per hour with product yields and carbon recoveries of 96% or greater. Although the substrate range of P. pastoris alcohol oxidase has been documented as C1–C5 aliphatic alcohols and benzyl alcohol, the use of a biphasic organic reaction medium showed that this enzyme can also oxidize higher molecular weight aliphatic alcohols of C6–C11, as well as the aromatic alcohols phenethyl alcohol and 3-phenyl-1-propanol. The ability of alcohol oxidase to oxidize low-water-soluble alcohols greatly extends the utility of this enzyme.Issued as NRCC no. 30955
Offprint requests to: W. D. Murray 相似文献
15.
Geoffrey K. Chambers John F. McDonald Michael McElfresh Francisco J. Ayala 《Biochemical genetics》1978,16(7-8):757-767
Starch and polyacrylamide gel electrophoresis were used to ascertain the substrate specificities of alcohol-oxidizing enzymes in 13 Drosophila species. The substrates used were a variety of long- and short-chain aliphatic alcohols, one aromatic alcohol, and benzaldehyde. Only one enzyme (product of a single-gene locus) showed significant NAD+-dependent alcohol dehydrogenase activity with short-chain aliphatic alcohols. The 13 species, belonging to four different Drosophila groups, all showed a similar complement of alcohol-oxidizing enzymes, although differences in electrophoretic mobility and in levels of activity existed from species to species. These findings are relevant to the adaptation of Drosophila to alcohol environments.This study was supported by NIH Grant 1 PO1 GM 22221 and by Contract PA 200-14 Mod #4 with ERDA. 相似文献
16.
We have found that in the alcoholic fermentation of amino acids by yeast isobutyl alcohol is produced from alanine and n-propyl and active amyl alcohols are formed from α-amino-n-butyric acid or threonine contrary to the F. Ehrlich’s scheme. These results suggest the close relationship among the formation of these higher alcohols and biosynthesis of valine from alanine and biosynthesis of isoleucine from α-amino-n-butyric acid or threonine.In this report, we studied the formation of n-propyl alcohol and active amyl alcohol from α-amino-n-butyric acid using washed yeast cells. 相似文献
17.
Dong-Pyo Hong Sung-Sik Lee Ryoichi Kuboi 《Journal of chromatography. B, Analytical technologies in the biomedical and life sciences》2000,743(1-2)
We examined quantitatively the effect of alcohols on protein and reverse micellar structure. We used circular dichroism (CD) to compare the effects of various alcohols on the protein structure, and percolation phenomena to evaluate the effects of various alcohols on reverse micellar structure. Upon the addition of alcohols to the bulk aqueous phase, proteins were denatured significantly, depending on the alcohol species and concentration, suggesting that use of alcohol directly to the stripping solution is not effective in back-extraction processes of proteins. In the present study, a new method, a small amount of alcohol is added to the surfactant–organic solution to improve the back-extraction behaviors of proteins. Practically, in the back-extraction process, the alcohols suppressing the cluster formation of reverse micelles (high value of βt), remarkably improved the back-extraction behavior of proteins. In addition, the same alcohol molecules showed a positive effect on the rate and fraction of protein back-extraction. From a result of the CD measurement of the back-extracted proteins, it was known that the alcohols added to reverse micellar solution allowed the proteins to back-extract safely without causing structural changes. These results show that the values of βt, defined by the variation of percolation processes, and the back-extraction behaviors of proteins have a good relationship, suggesting that the back-extraction processes were controlled by the micellar–micellar and protein–micellar interactions. 相似文献
18.
Biocatalytic asymmetric synthesis has been widely used for preparation of optically active chiral alcohols as the important intermediates and precursors of active pharmaceutical ingredients. However, the available whole-cell system involving anti-Prelog specific alcohol dehydrogenase is yet limited. A recombinant Escherichia coli system expressing anti-Prelog stereospecific alcohol dehydrogenase from Candida parapsilosis was established as a whole-cell system for catalyzing asymmetric reduction of aryl ketones to anti-Prelog configured alcohols. Using 2-hydroxyacetophenone as the substrate, reaction factors including pH, cell status, and substrate concentration had obvious impacts on the outcome of whole-cell biocatalysis, and xylose was found to be an available auxiliary substrate for intracellular cofactor regeneration, by which (S)-1-phenyl-1,2-ethanediol was achieved with an optical purity of 97%e.e. and yield of 89% under the substrate concentration of 5 g/L. Additionally, the feasibility of the recombinant cells toward different aryl ketones was investigated, and most of the corresponding chiral alcohol products were obtained with an optical purity over 95%e.e. Therefore, the whole-cell system involving recombinant stereospecific alcohol dehydrogenase was constructed as an efficient biocatalyst for highly enantioselective anti-Prelog synthesis of optically active aryl alcohols and would be promising in the pharmaceutical industry. 相似文献
19.
Alcohol dehydrogenase (ADH) and the genes encoding this enzyme have been studied intensively in a broad range of organisms. Little, however, has been reported on ADH in the free-living nematodeCaenorhabiditis elegans. Extracts of wild-typeC. elegans contain ADH activity and display a single band of activity on a native polyacrylamide gel. Reaction rate for alcohol oxidation is more rapid with higher molecular weight alcohols as substrate than with ethanol. Primary alcohols are preferred to secondary alcohols.C. elegans is sensitive to allyl alcohol, a compound that has been used to select for ADH-null mutants of several organisms. Allyl alcohol-resistant mutant strains were selected from ethylmethanesulfonate (EMS)-mutagenized nematode populations. ADH activity was measured in extracts from eight of these strains and was found to be low or nondetectable. These results form a basis for molecular and genetic characterization of ADH expression inC. elegans. 相似文献
20.
《Biocatalysis and Biotransformation》2013,31(3):191-212
Nicotinoprotein alcohol dehydrogenases are enzymes that contain non-dissociable NAD(P)(H) in the active site. The suitability of a nicotinoprotein alcohol dehydrogenase as coenzyme-independent alternative to classic alcohol dehydrogenases for enantioselective synthetic applications was studied. To this end the NADH-containing nicotinoprotein, np-ADH, from Rhodococcus erythropolis DSM 1069 was used as a model enzyme in different types of conversion: asymmetric synthesis, kinetic resolution and racemization. The enzyme was found to catalyze the asymmetric reduction of ketones using cheap reductants, such as ethanol, with high stereoselectivity, but the reaction was too slow to obtain good yields. Kinetic resolutions of racemic alcohols failed due to dismutation of the aldehyde that was used as cosubstrate. Racemization of a secondary alcohol via the corresponding ketone could not be achieved, which was due to an unidentified side reaction. This evaluation shows that, for developing biotransformations of industrial interest using nicotinoprotein alcohol dehydrogenases, the attention should be focused on enzymes with a higher reactivity towards prochiral ketones and secondary alcohols. 相似文献