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1.
M. Kataoka K. Shimizu K. Sakamoto H. Yamada S. Shimizu 《Applied microbiology and biotechnology》1995,44(3-4):333-338
A fungal lactonohydrolase catalyzes the stereospecific hydrolysis of the intramolecular ester bond of d-pantoyl lactone and is useful for optical resolution of racemic pantoyl lactone. High activity of this stereospecific hydrolysis reaction was found in several filamentous fungi belonging to the genera Fusarium, Gibberella and Cylindrocarpon through the screening in a variety of microorganisms. Fusarium oxysporum AKU 3702 showed high productivity of the enzyme and the cells containing the enzyme could be used repeatedly for this hydrolysis reaction. On incubation with the mycelia of this fungus, which had been cultivated in 3% glycerol, 0.5% Polypepton, 0.5% yeast extract and 0.5% corn steep liquor, pH 6.0, 46.0% of the racemic pantoyl lactone (700 mg/ml) was hydrolyzed and the optical purity of the pantoic acid formed was 96% enantiomeric excess for the d-isomer. 相似文献
2.
Honda K Tsuboi H Minetoki T Nose H Sakamoto K Kataoka M Shimizu S 《Applied microbiology and biotechnology》2005,66(5):520-526
The lactonase gene of Fusarium oxysporum was expressed in Aspergillus oryzae for optical resolution of dl-pantoyl lactone. When the chromosomal gene encoding the full-length form of the lactonase, which has its own NH2-terminal signal peptide, was introduced in the host cells, the resulting transformant produced an enzyme of 46,600 Da, which corresponded to the wild-type enzyme. In contrast, A. oryzae transformed with the cDNA coding the mature enzyme produced a protein of 41,300 Da. Deglycosylation analysis with an endoglycosidase revealed that the difference in molecular mass arose from the different sugar contents of the recombinant enzymes. The mycelia of the transformant were used as a catalyst for asymmetric hydrolysis of dl-pantoyl lactone. The initial velocity of the asymmetric hydrolysis reaction catalyzed by the transformant was estimated to be 30 times higher than that by F. oxysporum. When the mycelia of the transformant were incubated with a 20% dl-pantoyl lactone solution for 4 h, 49.9% of the racemic mixture was converted to d-pantoic acid (>95% ee). 相似文献
3.
Kohsuke Honda Michihiko Kataoka Sakayu Shimizu 《Biotechnology and Bioprocess Engineering》2002,7(3):130-137
Microbial lactonohydrolases (intramolecular ester bond-hydrolyzing enzymes) with unique properties were found. The lactonohydrolase
fromFusarium oxysporum catalyzes enantioselective hydrolysis of aldonate lactones andd-pantoyl lactone (d-PL). This enzyme is useful for the large-scale optical resolution of racemic PL. TheAgrobacterium tumefaciens enzyme catalyzes asymmetric hydrolysis of PL, but the stereospecificity is opposite to that of theFusarium enzyme. Dihydrocoumarin hydrolase (DHase) fromAcinetobacter calcoaceticus is a bifunctional enzyme, which catalyzes not only hydrolysis of aromatic lactones but also bromination of monochlorodimedon
in the presence of H2O2 and dihydrocoumarin. DHase also hydrolyzes several linear esters, and is useful for enantioselective hydrolysis of methyldl-β-acetylthioisobutyrate and regioselective hydrolysis of methyl cetraxate. 相似文献
4.
The ability of Aspergillus fumigatus
l-amino acid oxidase (l-aao) to cause the resolution of racemic mixtures of dl-amino acids was investigated with dl-alanine, dl-phenylalanine, dl-tyrosine, and dl-aspartic acid. A chiral column, Crownpak CR+ was used for the analysis of the amino acids. The enzyme was able to cause the
resolution of the three dl-amino acids resulting in the production of optically pure d-alanine (100% resolution), d-phenylalanine (80.2%), and d-tyrosine (84.1%), respectively. The optically pure d-amino acids have many uses and thus can be exploited industrially. This is the first report of the use of A. fumigatus
l-amino acid oxidase for racemic resolution of dl-amino acids. 相似文献
5.
E. Takahashi M. Furui Hiroyasu Seko T. Shibatani 《Applied microbiology and biotechnology》1997,47(2):173-179
The microbial degradation of l-methionine was investigated in order to develop a practical process for d-methionine production from racemic methionines. Among the 1000 culture strains tested, microorganisms belonging to the Achromobacter, Bacillus, Micrococcus, Morganella, Proteus, Providencia, Pseudomonas and Sarcina genera exhibited a high l-methionine-degrading activity. Proteus vulgaris IAM 12003 was determined to be the best strain and was used as a biocatalyst for eliminating the l-isomer. The degradation of l-isomer in this P. vulgaris IAM 12003 cell was assured by the action of l-amino acid oxidase. The maximum rate of l-isomer degradation was obtained at 30 °C and pH 8.0. Under these optimal conditions, the l-isomer in a 100 g/l mixture of racemic methionines was almost degraded within 20 h, with 46.5 g d-methionine/l remaining in the reaction mixture. Crystalline d-methionine, with a chemical purity greater than 99% and optical purity of 99.9% enantiomeric excess, was obtained at a yield
of 30% from the reaction mixture by simple purification.
Received: 17 June 1996 / Received last revision: 11 September 1996 / Accepted: 29 September 1996 相似文献
6.
Y. Tsuji H. Yamanaka T. Fukui T. Kawamoto A. Tanaka 《Applied microbiology and biotechnology》1997,47(2):114-119
In this paper we report on the enzymatic preparation of d-p-trimethylsilylphenylalanine (d-TMS-Phe). First, dl-5-(p-trimethylsilylphenylmethyl)hydantoin␣(dl-TMS-Phe-Hyd) was synthesized chemically and subjected to bacterial hydrolysis to obtain N-carbamoyl-d-p-trimethylsilylphenylalanine (C-d-TMS-Phe), but no strains examined showed sufficient hydantoinase activity on this compound. However, Blastobacter sp. A17p-4, which is known to produce N-carbamoyl-d-amino acid amidohydrolase (DCase), was found to be able to hydrolyze C-dl-TMS-Phe prepared chemically from the hydantoin. When C-dl-TMS-Phe was hydrolyzed with cells of Blastobacter sp. A17p-4, its optical purity was low because N-carbamoyl-l-amino acid amidohydrolase (LCase) coexisted in the cells. DCase and LCase in the cell-free extract of Blastobacter sp. A17p-4 could be separated by DEAE-Sephacel column chromatography. The optimum pH for the hydrolysis of C-dl-TMS-Phe by the partially purified DCase was 8.0 and addition of 2.5 % N,N-dimethylformamide was effective in raising the substrate concentration without inactivation of DCase. Under the optimized
conditions, highly optically pure (98 % enantiomeric excess) d-TMS-Phe could be obtained from C-dl-TMS-Phe with partially purified DCase.
Received: 12 July 1996 / Received revision: 11 September 1996 / Accepted: 2 November 1996 相似文献
7.
Tamura Kazumichi Sakazaki Riichi Kosako Yoshimasa Yoshizaki Etsuo 《Current microbiology》1986,13(4):179-184
The nameLeclercia adecarboxylata is proposed for a group of the family Enterobacteriacae previously known asEscherichia adecarboxylata. Leclercia adecarboxylata can be phenotypically differentiated from all other species of Enterobacteriaceae. The members of this species are positive for motility, indole production, methyl red, growth in the presence of KCN, malonate, beta-galactosidase, beta-xylosidase, esculin hydrolysis, gas production fromd-glucose, and acid production fromd-cellobiose,d-lactose, melibiose,l-rhamnose, adonitol,d-arabitol, dulcitol, and salicin; the strains were negative for Voges-Proskauer, citrate (Simmons), H2S (Kligler), lysine and ornithine decarboxylases, arginine dihydrolase, phenylalanine deaminase, gelatinase, DNase, Tween-80 hydrolysis, and acid production from myoinositol and alpha-methyl-d-glucoside. Fermentation ofd-raffinose,d-sucrose, andd-sorbitol is variable with strains. DNA relatedness of 11 strains ofL. adecarboxylata to three strains including the type strain of this species averaged 80% in reactions at 65°C. DNA relatedness to other species in Enterobacteriaceae was 2%–32%, indicating that this species was placed in a new genusLeclercia gen. nov. The type strain ofL. adecarboxylata is ATCC 23216. 相似文献
8.
Wang L Zhao B Li F Xu K Ma C Tao F Li Q Xu P 《Applied microbiology and biotechnology》2011,89(4):1009-1017
Highly efficient d-lactate production by Sporolactobacillus sp. strain CASD was demonstrated in this study. Peanut meal was found to be a better nutrient than yeast extract, soybean
meal, soybean peptone, corn steep, liquor beef extract, and ammonium sulfate in the production of d-lactate. To improve the utilization of peanut meal, the material was enzymatically hydrolyzed and simultaneously utilized
as the nitrogen source in d-lactate fermentation. Very high d-lactate production (207 g/L) was obtained using 40 g/L of peanut meal in 30-L fed-batch fermentation, with the average productivity
of 3.8 g/(L·h) and optical purity of 99.3%. The production of such a high concentration of optically pure d-lactate by strain CASD, with the simultaneous enzymatic hydrolysis of peanut meal and fermentation, represents a new cost-efficient
and integrated method for d-lactate production using agricultural by-products. 相似文献
9.
E. Takahashi M. Furui H. Seko T. Shibatani 《Applied microbiology and biotechnology》1997,47(4):347-351
In order to develop a practical process for d-lysine production from l-lysine, successive chemical racemization and microbial asymmetric degradation were investigated. The racemization of l-lysine proceeded quantitatively at elevated temperatures. A sample␣of 1000 strains of bacteria, fungi, yeast and actinomyces
were screened for the ability to degrade l-lysine asymmetrically. Microorganisms belonging to the Achromobacter, Agrobacterium, Candida, Comamonas, Flavobacterium, Proteus, Providencia, Pseudomonas and Yarrowia genera exhibited a high l-lysine-degrading activity. Comamonas testosteroni IAM 1048 was determined to be the best strain and used as a biocatalyst for eliminating the l isomer. The degradation rate of l-lysine with C. testosteroni IAM 1048 was influenced by pH, temperature and agitation speed. Under the optimal conditions, the l isomer in a 100-g/l mixture of racemic lysine was completely degraded within 72 h, with 47 g d-lysine/l left in the reaction mixture. Crystalline d-lysine, with a chemical purity greater than 99% and optical purity of 99.9% enantiomeric excess, was obtained at a yield
of 38% from the reaction mixture by simple purification. An engineering analysis of l-lysine racemization and microbial degradation was carried out to establish the basis of process design for d-lysine production.
Received: 24 September 1996 / Received last revision: 8 November 1996 / Accepted: 23 November 1996 相似文献
10.
Glucuronoyl esterase is a novel carbohydrate esterase recently discovered in the cellulolytic system of the wood-rotting fungus
Schizophyllum commune on the basis of its ability to hydrolyze methyl ester of 4-O-methyl-d-glucuronic acid. This substrate was not fully corresponding to the anticipated function of the enzyme to hydrolyze esters
between xylan-bound 4-O-methyl-d-glucuronic acid and lignin alcohols occurring in plant cell walls. In this work we showed that the enzyme was capable of
hydrolyzing two synthetic compounds that mimic the ester linkages described in lignin-carbohydrate complexes, esters of 4-O-methyl-d-glucuronic and d-glucuronic acid with 3-(4-methoxyphenyl)propyl alcohol. A comparison of kinetics of hydrolysis of methyl and 3-(4-methoxyphenyl)propyl
esters indicated that the glucuronoyl esterase recognizes the uronic acid part of the substrates better than the alcohol type.
The catalytic efficiency of the enzyme was much higher with the ester of 4-O-methyl-d-glucuronic acid than with that of d-glucuronic acid. Examination of the action of glucuronoyl esterase on a series of methyl esters of 4-O-methyl-d-glucopyranuronosyl residues α-1,2-linked to xylose and several xylooligosaccharides suggested that the rate of deesterification
is independent of the character of the carbohydrate part glycosylated by the 4-O-methyl-d-glucuronic acid. 相似文献
11.
A novel enzyme, l-carnitine amidase, was purified about 140-fold from a newly screened microorganism (DSM 6320) to yield a homogeneous protein. The native enzyme has a molecular mass of 125 kDa (gel filtration) and consists of two identical subunits as determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and Edman degradation. The pH optimum was found around pH 8.5. Out of 60 chemicals tested as substrates (amides of various aliphatic and aromatic acids, nitriles, amino acid amides and dipeptide amides) the amidase hydrolysed only l-carnitine amide. The Michaelis constant (Km) was found to be 11.6 mm, and the pure protein had a specific activity of 328 units/mg. Complex kinetics were observed with the racemic mixture of d,l-carnitine amide as starting material during enzymatic hydrolysis.
Correspondence to: M.-R. Kula 相似文献
12.
Tashiro Y Kaneko W Sun Y Shibata K Inokuma K Zendo T Sonomoto K 《Applied microbiology and biotechnology》2011,89(6):1741-1750
We isolated and characterized a d-lactic acid-producing lactic acid bacterium (d-LAB), identified as Lactobacillus delbrueckii subsp. lactis QU 41. When compared to Lactobacillus coryniformis subsp. torquens JCM 1166 T and L. delbrueckii subsp. lactis JCM 1248 T, which are also known as d-LAB, the QU 41 strain exhibited a high thermotolerance and produced d-lactic acid at temperatures of 50 °C and higher. In order to optimize the culture conditions of the QU 41 strain, we examined
the effects of pH control, temperature, neutralizing reagent, and initial glucose concentration on d-lactic acid production in batch cultures. It was found that the optimal production of 20.1 g/l d-lactic acid was acquired with high optical purity (>99.9% of d-lactic acid) in a pH 6.0-controlled batch culture, by adding ammonium hydroxide as a neutralizing reagent, at 43 °C in MRS
medium containing 20 g/l glucose. As a result of product inhibition and low cell density, continuous cultures were investigated
using a microfiltration membrane module to recycle flow-through cells in order to improve d-lactic acid productivity. At a dilution rate of 0.87 h−1, the high cell density continuous culture exhibited the highest d-lactic acid productivity of 18.0 g/l/h with a high yield (ca. 1.0 g/g consumed glucose) and a low residual glucose (<0.1 g/l)
in comparison with systems published to date. 相似文献
13.
Hiroshi Habe Tokuma Fukuoka Dai Kitamoto Keiji Sakaki 《Applied microbiology and biotechnology》2009,84(3):445-452
Glycerol is currently produced in large amounts as a by-product during fat splitting and biodiesel fuel production. Over the
past decade, both chemical and biotechnological processes to convert glycerol to value-added chemicals have been increasingly
explored. This mini-review provides recent information about the biotechnological production of a glycerol derivative, d-glyceric acid (d-GA), and its possible applications. Little is known about GA as a bioproduct, but it is naturally found in different kinds
of plants as a phytochemical constituent and is reported to have some biological activity. A racemic mixture of dl-GA can be obtained from glycerol via chemical oxidation; however, d-GA is mainly biotechnologically produced with the aid of bacteria. Under aerobic conditions, some acetic acid bacteria transform
glycerol into d-GA, and optimization of initial glycerol concentration and aeration rate provided a yield of more than 80 g/l d-GA, using a strain of Gluconobacter frateurii. 相似文献
14.
Mahendra Prasad 《Mycopathologia》1972,46(4):367-372
On the basis of sporulation (total output of all the three spore forms taken together) and fungal mat production bothF. oxysporum
Schlecht ex.Fr. andF. moniliforme v.subglutinans
Wr. &Rg. are auxoheterotrophic for thiamine, biotin, inositol, riboflavin and pyridoxine. The first three vitamins are selective in accelerating macro-conidial production also inF. moniliforme, which otherwise shows decrease with advance in days of incubation.F. moniliforme is an auxo-autotroph for nicotinic acid, Ca-pantothenate and folic acid and auxoheterotroph for ascorbic acid. Auxoautotrophy for Ca-pantothenate, folic acid, l-ascorbic acid and p-aminobenzoic acid cannot be suggested forF. oxysporum. Whereas nicotinic acid is a depressent of sporulation inF. oxysporum, inF. moniliforme another vitamin p-aminobenzoic acid depresses sporulation. As the two species ofFusarium show differences in preference as well as inhibition to at least five of the vitamins studied and also varied trends of pH changes exists there is full justification for their separate taxonomic placements. 相似文献
15.
Optically pure d-lactic acid was produced by fermentation of lactose with Lactobacillus bulgaricus Lb-12, and purified by crystallisation as magnesium d-lactate followed by extraction with butanol. The yield of d-lactate and contaminations with nitrogen and phosphorus were mapped during the purification procedure. The overall yield of d-lactic acid was 72% and the purity was more than 99%. Contaminations in the final d-lactic acid with nitrogen, phosphorus and l-lactic acid were only 0.032% w/w, 0.018% w/w and 0.04% w/w respectively. 相似文献
16.
J. Rath Robert Messner Paul Kosma Friedrich Altmann Leopold März Christian P. Kubicek 《Archives of microbiology》1995,164(6):414-419
A heteroglycan responsible for the binding of the enzyme β-1,4-d-glucosidase (EC 3.2.1.21) to fungal cell walls was isolated from cell walls of the filamentous fungusTrichoderma reesei. The heteroglycan, composed of mannose, galactose, glucose, and glucuronic acid, also activated β-1,4-d-glucosidase, β-1,4-d-xylosidase andN-acetyl-β-1,4-d-glucosaminidase activity in vitro. The structural backbone of this heteroglycan was prepared by acid hydrolysis and gel filtration.
The molecular structure of the core of the heteroglycan was determined by NMR studies as a linear α-1,6-d-mannan. The mannan core obtained by acid degradation stimulated the β-glucosidase activity by 90%. Several glycosidases fromAspergillus niger were also activated by theT. reesei heteroglycan. The β-glucosidase ofTrichoderma was activated by mannan fromSaccharomyces cerevisiae to a comparable extent. 相似文献
17.
The occurrence of a new bacterial dehalogenase acting on both the optical isomers of 2-halogenated alkanoic acids was demonstrated. When the haloalkanoic acid-utilizing bacteria were screened in a medium containing dl-2-chloropropionate as a sole carbon source, two types of bacteria were isolated: (1) a few strains utilizing both d- and l-isomers of 2-chloropropionate and (2) strains utilizing only the l-isomer. A dehalogenating enzyme was obtained from the cells of Pseudomonas sp. which is able to utilize both isomers. The crude enzyme catalyzed the dehalogenation of d- and l-2-chloropropionates to yield l- and d-isomers of lactate, respectively. The enzyme showed the same pH optimum and heat inactivation rate for the d- and l-isomers. Apparent K
m values for d- and l-2-chloropropionates were 4.5 and 1.0 mM, respectively. The enzyme acted specifically on 2-haloalkanoic acids. Activity staining of disc-gels electrophoresed witg the crude enzyme preparation showed that the dehalogenation of d- and l-2-chloropropionates, monochloroacetate, dichloroacetate, 2,2-dichloropropionate, and dl-2-chlorobutyrate is due to a single protein.Abbreviations MCA
monochloroacetic acid
- DCA
dichloroacetic acid
- TCA
trichloroacetic acid
- 2 MCPA
2-monochloropropionic acid
- 22 DCPA
2,2-dichloropropionic acid
- 3 MCPA
3-monochloropropionic acid
- 2 MCBA
2-monochlorobutyric acid
- 3 MCBA
3-monochlorobutyric acid
- 4 MCBA
4-monochlorobutyric acid 相似文献
18.
Okino S Suda M Fujikura K Inui M Yukawa H 《Applied microbiology and biotechnology》2008,78(3):449-454
In mineral salts medium under oxygen deprivation, Corynebacterium glutamicum exhibits high productivity of l-lactic acid accompanied with succinic and acetic acids. In taking advantage of this elevated productivity, C. glutamicum was genetically modified to produce d-lactic acid. The modification involved expression of fermentative d-lactate dehydrogenase (d-LDH)-encoding genes from Escherichia coli and Lactobacillus delbrueckii in l-lactate dehydrogenase (l-LDH)-encoding ldhA-null C. glutamicum mutants to yield strains C. glutamicum ΔldhA/pCRB201 and C. glutamicum ΔldhA/pCRB204, respectively. The productivity of C. glutamicum ΔldhA/pCRB204 was fivefold higher than that of C. glutamicum ΔldhA/pCRB201. By using C. glutamicum ΔldhA/pCRB204 cells packed to a high density in mineral salts medium, up to 1,336 mM (120 g l−1) of d-lactic acid of greater than 99.9% optical purity was produced within 30 h. 相似文献
19.
Zusammenfassung Das Murein (Peptidoglycan) eines aus Faeces isolierten Streptococcus, der in den wichtigsten Merkmalen mit Peptostreptococcus evolutus (Prevot) Smith übereinstimmt, weist folgende Molverhältnisse auf (aufgerundete bzw. abgerundete Zahlen): Mur:GlcNH2:Ala:Glu:Lys:Gly=1:1:3:1:1:1. Das Verhältnis l-Alanin:d-Alanin=2,15:1. Die Glutaminsäure liegt in der d-Konfiguration und als Amid vor.Durch die Partialhydrolyse der Zellwände und die anschließende Isolierung und Identifizierung der Peptide konnte die Aminosäuresequenz des Mureins geklärt werden. Das Tetrapeptid stimmt mit der üblichen Sequenz l-Ala-d-Glu-NH2-l-Lys-d-Ala der meisten übrigen Bakterien überein. Die Quervernetzung des Mureins wird durch das Peptid Glycyl-l-Alanin hergestellt, wobei l-Alanin an die -Aminogruppe des Lysins gebunden ist. Die Dinitrophenylierung der Zellwand ergab, daß 35% des Glycins und 6% des Lysins eine freie Aminogruppe aufweisen. Die Quervernetzung ist demnach nur zu höchstens 60% durchgeführt.
The chemical composition of the cell walls of Streptococci III. The amino acid sequence of a glycine containing murein from Peptostreptococcus evolutus (Prevot) Smith
Summary Peptostreptococcus evolutus was isolated from feces. Its murein containes muramic acid, glucosamine, alanine, d-glutamic acid, lysine and glycine at a molar ratio of about 1:1:3:1:1:1. The ratio of l-alanine: d-alanine is 2,15:1. Glutamic acid is present as an amide.By acid partial hydrolysis of the cell walls and subsequent isolation and identification of the peptides the amino acid sequence of the murein was elucidated. The tetrapeptide is identical with that of most bacteria (l-Ala-d-Glu-NH2-l-Lys-d-Ala). The crosslinking of the murein is performed by the peptide glycyl-l-alanine. l-alanine is attached to the -amino group of lysine while the amino group of glycine is bound to the carboxyl group of the c-terminal d-alanine of an adjacent tetrapeptide. About 35% glycine and 6% lysine of the murein are dinitrophenylisable indicating that maximally 60% of the possible cross-linkages are realized.相似文献
20.
Sergio Martínez-Rodríguez Ana Isabel Martínez-Gómez Felipe Rodríguez-Vico Josefa María Clemente-Jiménez Francisco Javier Las Heras-Vázquez 《Applied microbiology and biotechnology》2010,85(3):441-458
Enzymatic kinetic resolution is a widely used biotechnological tool for the production of enantiomerically pure/enriched compounds.
This technique takes advantage of the enantioselectivity or enantiospecificity of an enzyme for one of the enantiomers of
a racemic substrate to isolate the desired isomer. N-Carbamoyl-d- and l-amino acid amidohydrolases (d- and l-carbamoylases) are model enzymes for this procedure due to their strict enantiospecificity. Carbamoylase-based kinetic resolution
of amino acids has been applied for the last three decades, allowing the production of optically pure d- or l-amino acids. Furthermore, this enzyme has become crucial in the industrially used multienzymatic system known as “Hydantoinase
Process,” where the kinetic resolution produced by coupling an enantioselective hydantoinase and the enantiospecific carbamoylase
is enhanced by the enzymatic/chemical dynamic kinetic resolution of the low-rate hydrolyzed substrate. This review outlines
the properties of d- and l-carbamoylases, emphasizing their biochemical/structural characteristics and their biotechnological applications. It also
pinpoints new applications for the exploitation of carbamoylases over the forthcoming years. 相似文献