Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “ESTERASES”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 541 records · Page 30Linked to original sources
PubMed2000

Modifications of aclacinomycin T by aclacinomycin methyl esterase (RdmC) and aclacinomycin-10-hydroxylase (RdmB) from Streptomyces purpurascens.

The genes rdmB and rdmC of Streptomyces purpurascens encoding aclacinomycin modifying enzymes RdmB and RdmC were expressed in Streptomyces lividans TK24. In contrast to the earlier suggestion that RdmC may be an esterase that causes the removal of the carbomethoxy group from the 10 position of aclacinomycins, RdmC functions as an aclacinomycin methyl esterase and catalyzes the removal of the methoxy group from the C-15 position of aclacinomycin T producing 15-demethoxyaclacinomycin T. RdmB acts upon C-10 of 15-demethoxyaclacinomycin T and is able to remove the carboxylic group from the C-10 position. It functions also as an aclacinomycin-10-hydroxylase being able to add a hydroxyl group at the same, C-10 position in vitro. Aclacinomycin methyl esterase was purified to apparent homogeneity from S. lividans carrying the rdmC and aclacinomycin-10-hydroxylase as a glutathione S-transferase fusion construct from Escherichia coli carrying the rdmB gene, respectively. Aclacinomycin methyl esterase functions as a monomer and aclacinomycin-10-hydroxylase as a tetramer. Aclacinomycin methyl esterase has an exceptionally high temperature stability and has an apparent K(m) for aclacinomycin T of 15.5 microM. The introduction of rdmC and rdmB in a Streptomyces galilaeus mutant HO38 produced the same modifications of aclacinomycin T in vivo as aclacinomycin methyl esterase and aclacinomycin-10-hydroxylase in vitro.

Aclarubicin↗
PubMed2003

Enzymic release of reducing sugars from oat hulls by cellulase, as influenced by Aspergillus ferulic acid esterase and trichoderma xylanase.

Hydroxycinnamic acids, mainly ferulic and p-coumaric acids, are believed to be inhibitory to ruminal biodegradability of complex cell wall materials such as oat hulls. Previous studies have shown that a novel enzyme, Aspergillus ferulic acid esterase, and Trichoderma xylanase act synergistically to break the ester linkage between ferulic acid and the attached sugar of feruloyl polysaccharides, releasing ferulic acid from oat hulls. In this paper, we examined the enzymic release of reducing sugars from oat hulls by the actions of individual enzymes (Aspergillus ferulic acid esterase at 13 mU, 6.4 U, and 4678.4 U/assay; cellulase at 20 levels, ranging from 7.8 mU to 2772.7 U/assay; Trichoderma xylanase at 20 levels, ranging from 7.8 mU to 4096 U/assay) and by the combined action of cellulase at six levels (62.5 mU, 2 U, 16 U, 128 U, 1024 U, and 2772.7 U/assay), Aspergillus ferulic acid esterase at 13 mU/assay, and Trichoderma xylanase at two levels (1 U and 256 U/assay). The amount of total acid-extractable reducing sugars in the oat hulls used in this study was 793.8 +/- 8.0 microg/mg. The results show that after a 24-h incubation with Aspergillus ferulic acid esterase alone, no reducing sugars were observed to be released from oat hulls. With cellulase as the sole enzyme, as the concentration increased from 7.8 mU to 2772.7 U/assay, the release of reducing sugars increased (P < 0.01) from 0 to 39% of the total present, with the highest release at 512 U/assay. With Trichoderma xylanase alone, as the concentration increased from 7.8 mU to 4096 U/assay, the release of reducing sugars increased (P < 0.01) from 4.9 to 33%, with the highest release at 2048 U/assay. When incubated together with Trichoderma xylanase (1 U or 256 U/assay) and Aspergillus ferulic acid esterase (13 mU/assay), cellulase at all six levels (62.5 mU, 2 U, 16 U, 128 U, 1024 U and 2772.7 U/assay) significantly increased the release of reducing sugars (P < 0.01) from 8 to 69%. These results indicate that the synergistic interaction between Aspergillus ferulic acid esterase and Trichoderma xylanase on the release of ferulic acid from feruloyl polysaccharides of oat hulls makes the remainder of the polysaccharides open for further hydrolytic attack and facilitates the accessibility of the main chain of polysaccharides to cellulase. This action extends the cell wall hydrolysis, thus releasing a higher yield of reducing sugars. Such enzymic pretreatment of oat hulls may provide a unique advantage to rumen microorganisms for the biodegradation of the complex cell walls of byproduct feeds such as oat hulls.

Aspergillus↗
PubMed1993

Characterization of a B-type esterase involved in insecticide resistance from the mosquito Culex quinquefasciatus.

The enzyme, esterase B2, involved in insecticide resistance has been purified and characterized from the mosquito Culex quinquefasciatus. The monomeric enzyme has an M(r) of 62000 and a pI of 5.0. This enzyme is compared with the esterase A2 previously characterized [Ketterman, Jayawardena and Hemingway (1992) Biochem. J. 287, 355-360]. The kinetic constants for interaction with several insecticides indicate, as for the esterase A2, that the B2 enzyme has a role in resistance. The rates and affinities of binding observed support the hypothesis that the role mainly is sequestration followed by the slow turnover of the insecticide. Although the B2 esterase appears to have a slightly higher rate of interaction with insecticides, the A2 has a much greater Vmax. with the xenobiotic substrates studied. The B2 esterase also appears to be present in the larvae to a lesser extent than the esterase A2.

Animals↗
PubMed2000

Purification and characterization of an extracellular feruloyl esterase from the thermophilic anaerobe Clostridium stercorarium.

Feruloyl esterases act as accessory enzymes for the complete saccharification of plant cell wall hemicelluloses. Although many fungal feruloyl esterases have been purified and characterized, few bacterial phenolic acid esterases have been characterized. This study shows the extracellular production of a feruloyl esterase by the thermophilic anaerobe Clostridium stercorarium when grown on birchwood xylan. The feruloyl esterase was purified 500-fold in successive steps involving ultrafiltration, preparative isoelectric focusing and column chromatography by anion exchange, gel filtration and hydrophobic interaction. The purified enzyme released ferulic, rho-coumaric, caffeic and sinapinic acid from the respective methyl esters. The purified enzyme also released ferulic acid from a de-starched wheat bran preparation. At pH 8.0 and 65 degrees C, the Km and Vmax values for the hydrolysis of methyl ferulate were 0.04 mmol l-l and 131 micromol min-1 mg-1, respectively; the respective values for methyl coumarate were 0.86 mmol l-l and 18 micromol min-1 mg-1. The purified feruloyl esterase had an apparent mass of 33 kDa under denaturing conditions and showed optimum activity at pH 8.0 and 65 degrees C. At a concentration of 5 mmol l-l, the ions Ca2+, Cu2+, Co2+ and Mn2+ reduced the activity by 70-80%.

Anaerobiosis↗
PubMed2002

The EstA esterase is responsible for the main capacity of Lactococcus lactis to synthesize short chain fatty acid esters in vitro.

AIMS: Esters of short-chain fatty acids and alcohols participate significantly in the overall flavour of foods. The capacity of the lactic acid bacterium Lactococcus lactis to synthesize such esters is known even though the enzymes involved in the process are not well identified. The objective of our work is to determine whether the esterase is responsible for the whole capacity of L. lactis to synthesize esters in vitro. METHODS AND RESULTS: A negative mutant for the esterase was constructed and its capacity to synthesize short chain fatty acid esters from different substrate couples was compared to that of the wild type. We observed that the esterase is responsible for the main ester synthesis activity of L. lactis in vitro. However, in the presence of some substrates, the esterase negative mutant still synthesizes low amounts of esters. CONCLUSIONS: In favourable environmental conditions, the L. lactis esterase is responsible for the main ester synthesizing activity, even though another pathway for ester synthesis probably exists. SIGNIFICANCE AND IMPACT OF THE STUDY: Since esters are potent aroma compounds, esterase is probably a key enzyme in the development of food flavour.

Bacterial Proteins↗
PubMed2000

A modular esterase from Penicillium funiculosum which releases ferulic acid from plant cell walls and binds crystalline cellulose contains a carbohydrate binding module.

An esterase was isolated from cultures of the filamentous fungus Penicillium funiculosum grown on sugar beet pulp as the sole carbon source. The enzyme (ferulic acid esterase B, FAEB) was shown to be a cinnamoyl esterase (CE), efficiently releasing hydroxycinnamic acids from synthetic ester substrates and plant cell walls, and bound strongly to microcrystalline cellulose. A gene fragment was obtained by PCR using partial amino-acid sequences obtained from the pure enzyme and used to a probe a P. funiculosum genomic DNA library. A clone containing a 1120-bp ORF, faeB, was obtained which encoded a putative 353-residue preprotein including an 18-residue signal peptide, which when expressed in Eschericia coli produced CE activity. Northern analysis showed that transcription of faeB was tightly regulated, being stimulated by growth of the fungus on sugar beet pulp but inhibited by free glucose. The faeB promoter sequence contains putative motifs for binding an activator protein, XLNR, and a carbon catabolite repressor protein, CREA. FAEB was comprised of two distinct domains separated by a 20 residue Thr/Ser/Pro linker region. The N-terminal domain comprised 276 amino acids, contained a G-X-S-X-G motif typical of serine esterases, and was shown to be a member of a family comprising serine esterases, including microbial acetyl xylan esterases, poly (3-hydroxyalkanoate) depolymerases and CEs, and proteins of unknown function from Mycobacterium spp. and plants. The C-terminal domain comprised 39 amino acids and closely resembled the family 1 cellulose binding carbohydrate-binding modules (CBM) of fungal glycosyl hydrolases. This is the first report of a fungal CE with a CBM.

Amino Acid Sequence↗
PubMed1986

A sialic acid-specific O-acetylesterase in human erythrocytes: possible identity with esterase D, the genetic marker of retinoblastomas and Wilson disease.

The "nonspecific" esterases are a family of enzymes that were originally identified because of their reaction with synthetic O-acetyl ester substrates. While the electrophoretic polymorphisms of these enzymes have been extremely useful for genetic studies, their biological functions have remained completely unknown. Esterase D is characterized by its reactivity with 4-methylumbelliferyl acetate. This enzyme has recently been of particular interest because of its tight linkage to the putative recessive gene causing retinoblastomas, and to the recessive gene causing Wilson disease. We describe here the partial purification of a human erythrocyte esterase that appears to be highly specific for O-acetylated sialic acids. We next present evidence that suggests that esterase D is identical to this sialic acid-specific O-acetylesterase. First, both activities copurify from human erythrocyte lysates through several different purification steps, each of which use different principles of separation. Second, both activities show a remarkably similar profile of inhibition with a variety of different agents. Third, they both show a nearly identical heat-inactivation profile. This cytosolic sialic acid-specific O-acetylesterase appears to be involved in the "recycling" of O-acetylated sialic acid molecules. Thus, esterase D may be the first nonspecific esterase for which a specific biological role can be predicted.

Acetylesterase↗
PubMedDate not supplied

Characterization and expression of the prostatic arginine esterase gene, a canine glandular kallikrein.

The prostatic arginine esterase gene was isolated from a genomic library prepared with dog liver DNA in lambda EMBL3. The selected clone contained an insert of approximately 17 kb which included the whole coding portion of arginine esterase mRNA (5 exons plus 4 introns), 2 kb upstream from the initiation site and 12 kb downstream from the polyadenylation site. The intron-exon boundaries were identical to all known mammalian kallikrein genes. The deduced amino acid sequence indicated a high degree of identity (51-61%) with other kallikreins expressed not only in the prostate but also in the pancreas of various animal species. The 5'-flanking sequences contained potential regulatory elements such as a variant TATA box (TTTAAA), a CCAAT box, a SP1 transcriptional factor binding site (GGGCGG), and two TGTCCT motifs resembling glucocorticoid response elements. Southern blot analysis with an amplified cDNA fragment of 487 bp corresponding to the 5' portion of the mRNA and with a DNA probe from a different portion of the arginine esterase gene indicated the presence of two to three homologous genes in the canine genome while in a previous study a single band was detected using a 400-bp arginine esterase cDNA corresponding to the 3' portion of the mRNA. These results suggest that the arginine esterase gene belongs to a small kallikrein gene family. Arginine esterase mRNA is expressed primarily in the prostate but also at an extremely low level (approximately a thousandfold less) in several other tissues including the liver, the gracilis thigh muscle, the kidney, and the pancreas.

Animals↗
PubMed1992

Acute monocytic leukemia with chloroacetate esterase positivity. FAB M4 or M5?

French-American-British criteria for the diagnosis of acute monocytic leukemia (M5) require that 80% of nonerythroid bone marrow cells consist of monoblasts, promonocytes, and/or monocytes. Monocytic differentiation is demonstrated by fluoride-sensitive nonspecific esterase positivity. Chloroacetate esterase positivity is accepted as a marker of granulocytic differentiation. Three cases fulfilling French-American-British criteria for M5 showed fluoride-sensitive nonspecific esterase positivity in up to 100% of nonerythroid marrow cells but also exhibited strong chloroacetate esterase positivity in 20% to 90% of the same population. Less than 5% of blasts stained for Sudan black B and peroxidase. These cases may be viewed as chloroacetic esterase-positive acute monocytic leukemia or as acute myelomonocytic leukemia. The authors favor the former because the cases were myeloperoxidase negative; however, these cases indicate that chloroacetate esterase may not be a specific marker for granulocytic differentiation.

Aged↗
PubMed1990

Esterases A2 and B2 in Culex quinquefasciatus (Diptera: Culicidae): role in organophosphate resistance and linkage.

Two highly active esterases, A2 and B2, were isolated in SeLax, a strain of Culex quinquefasciatus Say from California which demonstrated resistance levels of 19, 14, and 4.3 times to the organophosphate insecticides chlorpyrifos, temephos, and malathion, respectively. Selection of SeLax by temephos during 31 generations increased resistance to this insecticide to 65 times. This resistance was shown to be DEF-suppressible, monofactorial, and strongly associated with the presence of esterases A2 and B2. Although these two esterases are encoded by distinct structural genes, no disjunction was observed when SeLax was crossed to S-Lab, a susceptible strain, or to S54, a strain resistant to organophosphates by means of esterase A1. However, when SeLax was crossed to strain Tem-R, which is resistant to organophosphates because of a highly active esterase B1, all possible recombinants occurred. These results were discussed in relation to the recent discovery that increased activity of B esterases in the genus Culex is caused by gene amplification.

Animals↗
PubMed1992

Adhesion Pad Formation and the Involvement of Cutinase and Esterases in the Attachment of Uredospores to the Host Cuticle.

We have investigated the basis of adhesion of uredospores of the obligately parasitic rust fungus Uromyces viciae-fabae to leaves of its broad bean host. Upon contact with an aqueous environment, spores form a structure that we have termed an adhesion pad. The adhesion pad is formed by both living and autoclaved spores, but only adhesion pads formed by living spores adhered to the cuticle of leaves of the host plant. Treatment of living spores with the serine-esterase inhibitor diisopropyl fluorophosphate prevented the adhesion of the pad to the leaf surface, suggesting a functional role for esterase or cutinase in the process of adhesion. A cutinase and two nonspecific serine-esterases were found to be localized on the surface of spores. These enzymes were released rapidly from the spore surface upon contact with an aqueous environment. The addition of the cutinase and the nonspecific esterases to autoclaved spores restored their ability to adhere to the host cuticle. Thus, whereas pad formation appears to be a passive response to the aqueous environment, the actual adhesion of pads to the host cuticle appears to depend on the cutinase and esterases associated with the spore surface. These results suggest a new role for cutinases and serine-esterases in the fungal infection process.

Journal Article↗
PubMed1989

N-alpha-benzyloxycarbonyl-L-lysine thiobenzyl ester (BLT) serine esterase in human cytolytic effector cells and cell line targets.

The granules of in vitro primed cytotoxic mouse T cells and cytotoxic cell lines have been shown to contain high levels of N-alpha-benzyloxycarbonyl-L-lysine thiobenzyl ester (BLT) esterase. The enzyme activity has been suggested to be associated with the cytotoxic capacity of killer cells. We investigated human leucocytes and found that neutrophils, monocytes, cytotoxic T lymphocytes (CTL), natural killer (NK) cells [large granular lymphocytes (LGL)], and interleukin 2 activated killer (LAK) cells, which all display efficient cytotoxic capacity, show only marginal BLT esterase activity. The low BLT esterase activity in human lymphocytes increases about twofold when cells are stimulated in vitro with interleukin 2 (IL-2), phytohaemagglutinin (PHA), or cultured in mixed lymphocyte culture (MLC). Mouse T lymphocytes have about 20 times more BLT esterase activity than human T lymphocytes. The BLT activity in mouse T cells also increases about twofold in MLC. The human leukaemia cell lines (K562, U937, MOLT-4, Jurkat) and the mouse mastocytoma line (P815), which are frequently used as target cells, contain more BLT esterase activity than human resting or activated lymphocytes. We did not find a direct correlation between the cytotoxic capacity and the BLT esterase activity of killer cells.

Animals↗
PubMed2006

Cell surface expression of bacterial esterase A by Saccharomyces cerevisiae and its enhancement by constitutive activation of the cellular unfolded protein response.

Yeast cell surface display is a powerful tool for expression and immobilization of biocatalytically active proteins on a unicellular eukaryote. Here bacterial carboxylesterase EstA from Burkholderia gladioli was covalently anchored into the cell wall of Saccharomyces cerevisiae by in-frame fusion to the endogenous yeast proteins Kre1p, Cwp2p, and Flo1p. When p-nitrophenyl acetate was used as a substrate, the esterase specific activities of yeast expressing the protein fusions were 103 mU mg(-1) protein for Kre1/EstA/Cwp2p and 72 mU mg(-1) protein for Kre1/EstA/Flo1p. In vivo cell wall targeting was confirmed by esterase solubilization after laminarinase treatment and immunofluorescence microscopy. EstA expression resulted in cell wall-associated esterase activities of 2.72 U mg(-1) protein for Kre1/EstA/Cwp2p and 1.27 U mg(-1) protein for Kre1/EstA/Flo1p. Furthermore, esterase display on the yeast cell surface enabled the cells to effectively grow on the esterase-dependent carbon source glycerol triacetate (Triacetin). In the case of Kre1/EstA/Flo1p, in vivo maturation within the yeast secretory pathway and final incorporation into the wall were further enhanced when there was constitutive activation of the unfolded protein response pathway. Our results demonstrate that esterase cell surface display in yeast, which, as shown here, is remarkably more effective than EstA surface display in Escherichia coli, can be further optimized by activating the protein folding machinery in the eukaryotic secretion pathway.

Bacterial Proteins↗
PubMed1988

Ferulic Acid Esterase Activity from Schizophyllum commune.

Schizophyllum commune produced an esterase which released ferulic acid from starch-free wheat bran and from a soluble ferulic acid-sugar ester that was isolated from wheat bran. The preferred growth substrate for the production of ferulic acid esterase was cellulose. Growth on xylan-containing substrates (oat spelt xylan and starch-free wheat bran) resulted in activity levels that were significantly lower than those observed in cultures grown on cellulose. Similar observations were made for endoglucanase, p-nitrophenyllactopyranosidase, xylanase, and acetyl xylan esterase. Of the enzymes studied, only arabinofuranosidase was produced at maximum levels during growth on xylan-containing materials. Ferulic acid esterase that had been partially purified by DEAE chromatography released significant amounts of ferulic acid from wheat bran only in the presence of a xylanase-rich fraction, indicating that the esterase may not be able to readily attack high-molecular-weight substrates. The esterase acted efficiently, without xylanase addition, on a soluble sugar-ferulic acid substrate.

Journal Article↗
PubMed1999

Characterization of an acetyl xylan esterase from the anaerobic fungus Orpinomyces sp. strain PC-2.

A 1,067-bp cDNA, designated axeA, coding for an acetyl xylan esterase (AxeA) was cloned from the anaerobic rumen fungus Orpinomyces sp. strain PC-2. The gene had an open reading frame of 939 bp encoding a polypeptide of 313 amino acid residues with a calculated mass of 34,845 Da. An active esterase using the original start codon of the cDNA was synthesized in Escherichia coli. Two active forms of the esterase were purified from recombinant E. coli cultures. The size difference of 8 amino acids was a result of cleavages at two different sites within the signal peptide. The enzyme released acetate from several acetylated substrates, including acetylated xylan. The activity toward acetylated xylan was tripled in the presence of recombinant xylanase A from the same fungus. Using p-nitrophenyl acetate as a substrate, the enzyme had a K(m) of 0.9 mM and a V(max) of 785 micromol min(-1) mg(-1). It had temperature and pH optima of 30 degrees C and 9.0, respectively. AxeA had 56% amino acid identity with BnaA, an acetyl xylan esterase of Neocallimastix patriciarum, but the Orpinomyces AxeA was devoid of a noncatalytic repeated peptide domain (NCRPD) found at the carboxy terminus of the Neocallimastix BnaA. The NCRPD found in many glycosyl hydrolases and esterases of anaerobic fungi has been postulated to function as a docking domain for cellulase-hemicellulase complexes, similar to the dockerin of the cellulosome of Clostridium thermocellum. The difference in domain structures indicated that the two highly similar esterases of Orpinomyces and Neocallimastix may be differently located, the former being a free enzyme and the latter being a component of a cellulase-hemicellulase complex. Sequence data indicate that AxeA and BnaA might represent a new family of hydrolases.

Acetylesterase↗
PubMed2000

Gene cloning and nucleotide sequencing and properties of a cocaine esterase from Rhodococcus sp. strain MB1.

A strain of Rhodococcus designated MB1, which was capable of utilizing cocaine as a sole source of carbon and nitrogen for growth, was isolated from rhizosphere soil of the tropane alkaloid-producing plant Erythroxylum coca. A cocaine esterase was found to initiate degradation of cocaine, which was hydrolyzed to ecgonine methyl ester and benzoate; both of these esterolytic products were further metabolized by Rhodococcus sp. strain MB1. The structural gene encoding a cocaine esterase, designated cocE, was cloned from Rhodococcus sp. strain MB1 genomic libraries by screening recombinant strains of Rhodococcus erythropolis CW25 for growth on cocaine. The nucleotide sequence of cocE corresponded to an open reading frame of 1,724 bp that codes for a protein of 574 amino acids. The amino acid sequence of cocaine esterase has a region of similarity with the active serine consensus of X-prolyl dipeptidyl aminopeptidases, suggesting that the cocaine esterase is a serine esterase. The cocE coding sequence was subcloned into the pCFX1 expression plasmid and expressed in Escherichia coli. The recombinant cocaine esterase was purified to apparent homogeneity and was found to be monomeric, with an M(r) of approximately 65,000. The apparent K(m) of the enzyme (mean +/- standard deviation) for cocaine was measured as 1.33 +/- 0.085 mM. These findings are of potential use in the development of a linked assay for the detection of illicit cocaine.

Amino Acid Sequence↗
PubMed1977

Isolation of acetyl esterase mutants of Bacillus subtilis 168.

Five mutants of Bacillus subtilis 168 defective in an intracellular esterase activity were identified. By polyacrylamide gel electrophoresis, four of the mutants were shown to lack esterase B activity, and the fifth lacked esterase A activity. All of the back-crossed esterase mutants were able to sporulate at wild-type frequency and produce exoprotease(s) and antibiotic(s). No difference in motility could be attributed to the esterase mutation. PBS1 transduction analysis showed all the esterase B mutations to be linked to the hisA marker.

Acetylesterase↗
PubMed1997

Isolation, analysis, and expression of two genes from Thermoanaerobacterium sp. strain JW/SL YS485: a beta-xylosidase and a novel acetyl xylan esterase with cephalosporin C deacetylase activity.

The genes encoding acetyl xylan esterase 1 (axe1) and a beta-xylosidase (xylB) have been cloned and sequenced from Thermoanaerobacterium sp. strain JW/SL YS485. axe1 is located 22 nucleotides 3' of the xylB sequence. The identity of axe1 was confirmed by comparison of the deduced amino acid sequence to peptide sequence analysis data from purified acetyl xylan esterase 1. The xylB gene was identified by expression cloning and by sequence homology to known beta-xylosidases. Plasmids which independently expressed either acetyl xylan esterase 1 (pAct1BK) or beta-xylosidase (pXylo-1.1) were constructed in Escherichia coli. Plasmid pXylAct-1 contained both genes joined at a unique EcoRI site and expressed both activities. Substrate specificity, pH, and temperature optima were determined for partially purified recombinant acetyl xylan esterase 1 and for crude recombinant beta-xylosidase. Similarity searches showed that the axe1 and xylB genes were homologs of the ORF-1 and xynB genes, respectively, isolated from Thermoanaerobacterium saccharolyticum. Although the deduced sequence of the axe1 product had no significant amino acid sequence similarity to any reported acetyl xylan esterase sequence, it did have strong similarity to cephalosporin C deacetylase from Bacillus subtilis. Recombinant acetyl xylan esterase 1 was found to have thermostable deacetylase activity towards a number of acetylated substrates, including cephalosporin C and 7-aminocephalosporanic acid.

Acetylesterase↗