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PubMed1975

Inhibition of thiamine transport in anaerobic baker's yeast by iodoacetate, 2,4-dinitrophenol N,N'-dicyclohexylcarbodiimide and fatty acids.

1. [14C]Thiamine uptake by baker's yeast (Saccharomyces cerevisiae) was strongly inhibited by 0.2 mM iodoacetate, 0.2 mM 2,4-dinitrophenol and 0.1 mM N,N'-dicyclohexylcarbodiimide under anaerobic conditions. 2. The inhibition of anaerobic [14C]thiamine uptake by these inhibitors was accompanied by almost parallel decreases in the ATP level of the yeast cells. 3. On the other hand, the short-chain fatty acids inhibited [14C]thiamine uptake to a large extent, without greatly affecting the intracellular ATP level. This suggests that the acids primarily block the use of energy from ATP for the transport rather than the fermentation process. 4. Caproate, which has a most pronounced inhibitory effect on [14C]thiamine uptake, significantly prevented the dissipation of an energized membrane state of yeast cells necessary for the active transport of thiamine. 5. Possible ways in which the inhibitors may affect thiamine uptake were discussed.

Adenosine Triphosphate↗

PubMed1987

Occurrence, absorption and metabolism of short chain fatty acids in the digestive tract of mammals.

Short chain fatty acids (SCFA) also named volatile fatty acids, mainly acetate, propionate and butyrate, are the major end-products of the microbial digestion of carbohydrates in the alimentary canal. The highest concentrations are observed in the forestomach of the ruminants and in the large intestine (caecum and colon) of all the mammals. Butyrate and caproate released by action of gastric lipase on bovine milk triacylglycerols ingested by preruminants or infants are of nutritional importance too. Both squamous stratified mucosa of rumen and columnar simple epithelium of intestine absorb readily SCFA. The mechanisms of SCFA absorption are incompletely known. Passive diffusion of the unionized form across the cell membrane is currently admitted. In the lumen, the necessary protonation of SCFA anions could come first from the hydration of CO2. The ubiquitous cell membrane process of Na+-H+ exchange can also supply luminal protons. Evidence for an acid microclimate (pH = 5.8-6.8) suitable for SCFA-protonation on the surface of the intestinal lining has been provided recently. This microclimate would be generated by an epithelial secretion of H+ ions and would be protected by the mucus coating from the variable pH of luminal contents. Part of the absorbed SCFA does not reach plasma because it is metabolized in the gastrointestinal wall. Acetate incorporation in mucosal higher lipids is well-known. However, the preponderant metabolic pathway for all the SCFA is catabolism to CO2 except in the rumen wall where about 80% of butyrate is converted to ketone bodies which afterwards flow into bloodstream. Thus, SCFA are an important energy source for the gut mucosa itself.

Animals↗

PubMed1981

A direct method to assay neurotoxic esterase activity.

A direct photometric method for assaying neurotoxic esterase (NTE) activity of chicken brain microsomal preparation has been developed using 4-nitrophenyl esters as substrates. Paired samples of the microsomal preparation were preincubated for 20 min with paraoxon plus either (a) buffer or (b) mipafox before addition of substrate. The initial rate of NTE activity was directly recorded at 410 nm by matching the content of tube (a) against tube (b) after addition of the substrate to both of them. The 4-nitrophenyl esters of propionic, butyric, valeric, lauric, capric and caproic acids were tested as substrates. Results indicated that 4-nitrophenyl valerate and caproate, respectively, are the most hydrolyzable substrates for NTE with this method; its also enables detailed kinetic studies of NTE to be made. The Michaelis constant (Km) for the hydrolysis of 4-nitrophenyl valerate by NTe was found to be 5.55 . 10(-5) M.

Animals↗

PubMed1988

Enzymatic characterization of three aeromonas species using API Peptidase, API "Osidase," and API Esterase test kits.

An enzymatic characterization of 16 strains of Aeromonas species including A. hydrophila (7), A. sobria (5), and A. caviae (4) was carried out using API Peptidase (strips numbered 1, 2, 3, 4, 5, and 6); API Esterase and API "Osidase" test strips. A total of 89 substrates was used in the assay and included 59 arylamides (aminopeptides), 10 esters, and 20 carbohydrates. All three species were remarkably uniform in their reactivities. Nineteen (32%) of the arylamide substrates used were hydrolyzed by all three species. Very strong arylamidase activity was displayed by all three species for L-lysine, L-hydroxyproline, L-arginine, L-alanine, L-proline, and L-leucyl-L-alanine. Esterase activity was strongest against caproate (C6), caprylate (C8), nonanoate (C9), and caprate (C10) substrates. Only a limited number of carbohydrate substrates were hydrolyzed; strong N-acetyl-beta-D-glucosaminidase activity was given by all strains. Both A. hydrophila and A. caviae gave strong beta-D-glucosidase reactivities, while A. sobria appeared to be negative for this enzyme. The results of our preliminary study show that some of the enzymes examined may be useful in the identification and differentiation of these species. The API enzyme assays yielded rapid (4 hr) results. The assays were easy to perform, relatively inexpensive and reproducible. The importance of replicate testing and the inclusion of uninoculated (buffer only) controls as part of the assay is emphasized.

Aeromonas↗

PubMed2006

A primer on antenatal testing for neonatal nurses: part 1. Tests used to predict preterm labor.

Parents and healthcare providers are challenged to understand the mechanisms of, and predictors for preterm delivery. In addition to the epidemiologic implications, on a practical level, the ability to predict preterm delivery may help the neonatal team triage to assure bed availability, and to predict and provide appropriate staffing for new admissions. On an individual patient level, understanding the maternal history, including antenatal risk factors and relevant monitoring and testing, is an important foundation for subsequent neonatal care. A number of new diagnostic testing tools are being used in obstetric practice to enhance the ability to predict preterm delivery. The results of fetal fibronectin and ultrasound measurement of cervical length are increasingly used to triage obstetrical patients. Results of these tests may prompt transfer to a tertiary facility. Part 1 of this 2-part series will describe antenatal testing techniques used to predict preterm delivery (PTD), as well as highlight the emerging developments in maternal serum testing. Further, a recent treatment option for preterm labor, 17 alpha-hydroxyprogesterone caproate, will also be discussed.

Female↗

PubMed2005

Plasma CRH measurement at 16 to 20 weeks' gestation does not predict preterm delivery in women at high-risk for preterm delivery.

OBJECTIVE: The purpose of this study was to examine the utility of a single second-trimester plasma corticotropin-releasing hormone measurement as a marker for preterm delivery in women at high risk for preterm delivery. STUDY DESIGN: This is an analysis of data from a multicenter placebo-controlled trial designed to evaluate the role of 17 alpha hydroxyprogesterone caproate (17P) in the prevention of recurrent preterm birth. Women with a documented history of a previous spontaneous preterm birth at <37 weeks were enrolled (16-20 wks) and randomly assigned in a 2 to 1 ratio to weekly injections of 17P or matching placebo. Blood was collected before treatment in 170 patients (113 assigned 17P and 57 placebo) who were enrolled at 11 of the 19 centers. Plasma levels of corticotropin-releasing hormone were compared between those who delivered preterm and those delivering at term. Data were analyzed using the Wilcoxon rank-sum test. RESULTS: The overall rates of preterm birth in this cohort of 170 patients were 35.9% at <37 weeks (31.9% progesterone, 43.9% placebo), and 19.4% at <35 weeks (18.6% vs 21.1%). The median levels of corticotropin-releasing hormone were similar between those delivering at <37 weeks and those delivering > or = 37 weeks (0.39 ng/mL vs 0.37 ng/mL, P = .08). In addition, there were no differences in corticotropin-releasing hormone levels among those who delivered at <35 weeks or > or = 35 weeks (0.36 vs 0.38, P = .90). Moreover, there were no differences in corticotropin-releasing hormone levels among those in the placebo group who delivered at <37 or > or = 37 weeks (0.40 vs 0.41, P = .72) and at <35 or > or = 35 weeks (P = .64). CONCLUSION: A single measurement of corticotropin-releasing hormone at 16 to 20 weeks' gestation is not a good biomarker for recurrent preterm delivery in patients at high risk for this complication.

Adult↗

PubMed2004

Sequence-based approach to finding functional lipases from microbial genome databases.

A sequence-based approach was used to retrieve functional lipases from microbial genome databases. Many novel genes assigned as putative lipases were tested using the criteria of the typical lipase sequence rule, based on a consensus sequence of a catalytic triad (Ser, Asp, His) and oxyanion hole sequence (HG). To obtain the lipase genes satisfying the sequence rule, PCR cloning was performed, while the lipase activities were tested using a tributyrin/tricaprylin plate and p-nitrophenyl caproate. Among nine putative lipases from four strains, five functional lipolytic proteins were obtained from Archaeoglobus fulgidus, Deinococcus radiodurans, and Agrobacterium tumefaciens. All five lipases exhibited a relatively low sequence similarity (less than 26.7%) with known lipases and turned out to belong to different lipase families. Accordingly, the current results indicate that the proposed strategic approach based on the microbial genome is an efficient and rapid method for finding novel and functional lipases.

Agrobacterium tumefaciens↗

PubMed2004

A novel thermostable esterase from the thermoacidophilic archaeon Sulfolobus tokodaii strain 7.

We have characterized an esterase expressed from the putative esterase gene (ST0071) selected from the total genome analysis from the thermoacidophilic archaeon Sulfolobus tokodaii strain 7. The ORF was cloned and expressed as a fusion protein in Escherichia coli. The protein was purified with heat treatment, affinity column chromatography, and size exclusion filtration. The optimum activity for ester cleavage against p-nitrophenyl esters was observed at around 70 degrees C and pH 7.5-8.0. The enzyme exhibited high thermostability and also showed activity in a mixture of a buffer and water-miscible organic solvents, such as acetonitrile and dimethyl sulfoxide. From the kinetic analysis, p-nitrophenyl butyrate was found to be a better substrate than caproate and caprylate.

Cloning, Molecular↗

PubMed2005

Identification and characterisation of LIP7 and LIP8 genes encoding two extracellular triacylglycerol lipases in the yeast Yarrowia lipolytica.

In the lipolytic yeast Yarrowia lipolytica, the LIP2 gene was previously reported to encode an extracellular lipase. The growth of a Deltalip2 strain on triglycerides as sole carbon source suggest an alternative pathway for triglycerides utilisation in this yeast. Here, we describe the isolation and the characterisation of the LIP7 and LIP8 genes which were found to encode a 366 and a 371-amino acid precursor protein, respectively. These proteins which belong to the triacylglycerol hydrolase family (EC 3.1.1.3) presented a high homology with the extracellular lipase CdLIP2 and CdLIP3 from Candida deformans. The physiological function of the lipase isoenzymes was investigated by creating single and multi-disrupted strains. Lip7p and Lip8p were found to correspond to active secreted lipases. The lack of lipase production in a Deltalip2 Deltalip7 Deltalip8 strain suggest that no additional extracellular lipase remains to be discovered in Y. lipolytica. The substrate specificity towards synthetic ester molecules indicates that Lip7p presented a maximum activity centred on caproate (C6) while that of Lip8p is in caprate (C10).

Amino Acid Sequence↗

PubMed2004

Molecular cloning and characterization of two thermostable carboxyl esterases from Geobacillus stearothermophilus.

Screening of the genomic libraries of Geobacillus stearothermophilus ATCC12980 and ATCC7954 for esterase/lipase activity led to the isolation of two positive clones. The results of subclonings and sequence analyses identified two genes, est30 and est55, encoding two different carboxylesterases, and genetic rearrangement in the est55 locus was revealed from genomic comparison. The est30 gene encodes a polypeptide of 248 amino acids with a calculated molecular mass of 28338 Da, and the est55 gene encodes a polypeptide of 499 amino acids with a calculated molecular mass of 54867 Da. Both enzymes were purified to near homogeneity from recombinant strains of Escherichia coli. The results of enzyme characterization showed that while both enzymes possess optimal activities with short chain acyl derivatives, Est55 has a broader pH tolerance (pH 8-9) and optimal temperature range (30-60 degrees C) than Est30. The activation energy of Est55 (35.7 kJ/mol) was found to be significantly lower than that of Est30 (101.9 kJ/mol). Both enzymes were stable at 60 degrees C for more than 2 h; at 70 degrees C, the half-life for thermal inactivation was 40 and 180 min for Est55 and Est30, respectively. With p-nitrophenyl caproate as the substrate and assayed at 60 degrees C, Est55 had K(m) and k(cat) values of 0.5 microM and 39758 s(-1) while Est30 exhibited values of 2.16 microM and 38 s(-1). Inhibition studies indicated that both Est30 and Est55 were strongly inhibited by phenylmethanesulfonyl fluoride, p-hydroxymercuribenzoate, and tosyl-l-phenylalanine, consistent with the proposed presence of Ser-His-Glu catalytic triad of the alpha/beta hydrolase family. The enzymatic properties of Est30 and Est55 reported here warrant the potential applications of these enzymes in biotechnological industries.

Carboxylic Ester Hydrolases↗

PubMed2006

Anaerobic treatment of phenol in wastewater under thermophilic condition.

Over 99% of phenol was effectively degraded in an upflow anaerobic sludge blanket (UASB) reactor at 55 degrees C with 40 h of hydraulic retention time (HRT) for a wastewater containing 630 mg/L of phenol, corresponding to 1500 mg/L of chemical oxygen demand (COD) and a loading rate of 0.9 g-COD/L/d. The maximum specific methanogenic activity (SMA) of the phenol-degrading sludge was 0.09 g-CH4-COD/g-volatile suspended solids (VSS)/d. Based on 16S rDNA analysis, a total of 21 operational taxonomy units (OTUs) were found in the sludge, of which eight (42.6% of the total population) were related to the sequences in the GenBank with similarity of over 97%, and 13 (79.6%) were affiliated with the known thermophilic species. Additional SMA data and phylogenetic analysis suggest that the degradation pathway of phenol for thermophilic sludge was likely via caproate, instead of benzoate as for the mesophilic sludge.

Bacteria, Anaerobic↗

PubMed2002

Enhancement of NGF- and cholera toxin-induced neurite outgrowth by butyrate in PC12 cells.

It has been shown that sodium butyrate (NaBu) does not elicit neurite outgrowth of PC12, one of the most widely used cell lines as a model of neuronal differentiation. In this study, the effects of NaBu on nerve growth factor (NGF)- and cholera toxin-induced neurite outgrowth in PC12 cells were examined. NaBu dose-dependently enhanced neurite formation induced by both agents. The maximum responses obtained at 0.5 mM NaBu were nearly twice those of the inducers alone. Propionate and valerate were also effective, but acetate and caproate were ineffective. Among the butyrate analogs with a moiety of three to five carbon atoms tested, isobutyrate, isovalerate, vinylacetate and 3-chloropropionate enhanced neurite outgrowth promoted by both inducers. However, neither alpha-, beta-, and gamma-aminobutyrates nor alpha-, beta-, and gamma-hydroxybutyrates were effective. All of the effective short-chain fatty acids and their analogs increased the level of histone acetylation, while ineffective ones did not. Furthermore, Helminthosporium carbonum toxin (HC toxin), a structurally dissimilar inhibitor of histone deacetylase, mimicked the effect of butyrate. These results suggest that NaBu enhances neurite outgrowth induced by NGF and cholera toxin in PC12 cells through a mechanism involving an increase in the level of histone acetylation.

Acetylation↗

PubMed2003

Fatty acids as an energy source for the operation of axoplasmic transport.

Fatty acids are utilized as a cellular energy source. In the present study, we investigated whether fatty acids could affect axoplasmic transport. Cultured mouse superior cervical ganglion neurons were placed in the glucose-containing medium (145 mM NaCl, 5 mM KCl, 1 mM CaCl(2), 1 mM MgCl(2), 5 mM D-glucose, 10 mM Hepes, pH 7.3, 37 degrees C), and axoplasmic transport of particles in neurites was observed under video-enhanced contrast microscopy. A variety of fatty acids (acetate (C2), caproate (C6), caprylate (C8), caprate (C10), 2-decenoate (C10:1), arachidonate (C20:4); 0.1-1 mM) caused a transient increase in the amount of particles transported in both anterograde and retrograde directions. The increasing effects of fatty acids were dose-dependent. A half-maximum effective dose (ED(50)) for acetate was 0.8 mM, which is similar to the reported K(m) value of acetyl-CoA synthetase for acetate. The ED(50) for caprylate was 28 microM, which is near the K(m) value of acyl-CoA synthetase for medium- and long-chain fatty acids. Application of 5 mM malonate, an inhibitor of the citrate cycle, induced a steady-state decrease in axoplasmic transport, indicating that energy derived from the citrate cycle is required for the maintenance of axoplasmic transport. The increasing effect of acetate (1 mM) on axoplasmic transport was completely abolished by pretreatment with malonate (5 mM), suggesting that acetate produces ATP for axoplasmic transport via the citrate cycle. Alternatively, the effect of caprate (1 mM) was retained after treatment with malonate. Thus, fatty acids except acetate produce ATP probably through both the beta-oxidation pathway and the citrate cycle, increasing axoplasmic transport. Since the effect of fatty acids was transient, certain negative feedback mechanisms might be involved. The removal of glucose from the medium resulted in a low steady-state level of axoplasmic transport. Under such condition, the acetate (1 mM)-induced transient increase in axoplasmic transport remained. Since intracellular ATP must be low under glucose-free condition, intracellular ATP concentrations are unlikely to be involved in the feedback system. Instead, acetyl-CoA or its downstream products in the citrate cycle might lead to feedback inhibition. Application of citrate (5 mM) caused a strong decrease following a transient increase in axoplasmic transport, whereas no other acetyl-CoA product decreased axoplasmic transport. Thus, excessive citrate may be one of factors leading to feedback inhibition of metabolic pathways to arrest and reverse the increase in axoplasmic transport induced by fatty acids.

Animals↗

PubMed1997

Synthesis and mass spectrometric characterization of digoxigenin and biotin labeled ganglioside GM1 and their uptake by and metabolism in cultured cells.

Selective acylation of mono-deacetyl lyso-GM1, i.e. beta-D-galactopyranosyl-(1-->3)-2-acetamido-2-deoxy-beta-D-galactopyr ano syl -(1-->4)-(alpha-D-neuraminyl-(2-->3))-beta-D-galactopyranosyl- (1-->4)-beta-D-glucopyranosyl-(1-->1)-(2S,3R,4E)-2-amino-4-octa decen-1,3-diol, with N-succinimidyl-[1-14C]stearate afforded labeled mono-deacetyl GM1, i.e. beta-D-galactopyranosyl-(1-->3)-2-acetamido-2-deoxy-beta-D-galactopyr ano syl- (1-->4)-(alpha-D-neuraminyl-(2-->3)-beta-D-galactopyranosyl-(1-->4)-beta -D- glucopyranosyl-(1-->1)-(2S,3R,4E)-2-[1-14C]octadecanamido-4- octadecen-1, 3-diol, in good yield. Its condensation with either N-succinimidyl-digoxigenyl-3-O-methyl carbonyl-epsilon-amino caproate or N-succinimidyl-D-biotinyl-epsilon-aminocaproate led to radioactive GM1 derivatives carrying a tag for immuno-electron microscopy at the sialic acid residue. These GM1 derivatives could be hydrolyzed to the corresponding GM3 derivatives by treatment with GM1-beta-galactosidase and beta-hexosaminidases. There was no further degradation by sialidases due to the bulky tag in the sialic acid residue. The uptake of biotin labeled GM1 by human skin fibroblasts, rat neuroblastoma cells B104 and human neuroblastoma cells SHSY5Y was 0.85, 0.58 and 1.62 nmol lipid/mg cellular protein, respectively, after an incubation for 66 h at 37 degrees C and was similar to that of untagged GM1. The uptake of digoxigenin labeled GM1 by these cell types was, however, significantly higher (3.1, 6.8, and 20.0 nmol lipid/mg cellular protein, respectively). Both the biotin and digoxigenin labeled GM1 analogs were catabolized to the corresponding GM2 and GM3 derivatives in lysosomes of cultured cells. This demonstrates that these synthetic analogues are suitable for studying, by immuno-electron microscopy, their endocytosis and distribution in intralysosomal membranes.

Biotin↗

PubMed1977

[Thin-layer chromatography of active compounds from ointments and suppositories followed by direct quantitative analysis by remission (author's transl)].

The paper describes a method for simultaneous thin-layer chromatographic separation of hydrocortisone, hydrocortisone acetate or hydrocortisone caproate alongside dibucaine hydrochloride, hexachlorophene and clemizole undecylate as well as clemizole hexachlorophenate in ointments and suppositories. Development of thin-layer chromatograms is carried out on silica gel 60 F-254 pre-coated plates. All four active ingredients can be separated on one silica gel plate using one solvent system and determined directly by the remission method using a densitometer. Hydrocortisone and its two esters are measured at 248 nm, dibucaine hydrochloride at 325 nm, hexachlorophene at 300 nm, and clemizole undecylate as well as clemizole hexachlorophenate at 275 nm. Evaluation of thin-layer chromatograms takes place on-line from a linear calibration curve using an IBM 1800 computer. The described method is very suitable for analyses of these active ingredients in drug forms, such as ointments or suppositories and is reproducible with coefficients of variation of 1.29-3.56%.

Benzimidazoles↗

PubMed1983

Formation and properties of a covalent complex between elongation factor Tu and Phe-tRNA bearing a photoaffinity probe on its 3-(3-amino-3-carboxypropyl)uridine residue.

Escherichia coli Phe-tRNA, modified with the photoaffinity reagent 6-(2-nitro-4-azidophenylamino)caproate on the 3-(3-amino-3-carboxypropyl)uridine residue, was crosslinked to E. coli EFTu Section upon irradiation at 0 degree C with visible light at wavelengths greater than 400 nm. Crosslinking was dependent on irradiation, the photoaffinity probe, and was blocked by pre-photolysis. 1 mM-dithiothreitol completely quenched crosslinking. Binding of the tRNA to EFTu was a prerequisite for crosslinking, because neither EFTu . GDP nor AcPhe-tRNA could substitute; EFTu . GDPCP, however, was almost as active as EFTu . GTP. Crosslinking was complete in less than five minutes and was stable to at least 20 minutes of irradiation with a single 650 W tungsten lamp 4 cm away. The crosslinking yield ranged from 15% to 25%. The crosslinked complex possessed several remarkable properties. At 0.5 mM-Mg2+, the complex protected the AA-tRNA link to chemical hydrolysis, stabilized the bound GTP to dissociation or exchange, and was not adsorbed to cellulose nitrate filters. The purified crosslinked complex could be bound to ribosomes with concomitant hydrolysis of GTP. Extensive peptide bond formation with AcPhe-tRNA in the P site occurred despite the presence of the crosslinked EFTu. We conclude that hydrolysis of GTP is sufficient to release the 3' end of the Phe-tRNA from complexation with EFTu. Translocation of the A site bound complex did not occur. The crosslink site on EFTu is probably near the periphery of the molecule, because shortening the probe from 20 A to 14 A completely blocked crosslinking. A similar but shorter 8 A probe, p-azidophenacyl-4-thiouridine located on the opposite face of the tRNA, did not crosslink.

Affinity Labels↗

PubMed1997

Characterisation of the two malate dehydrogenases from Phytomonas sp. Purification of the glycosomal isoenzyme.

Two NAD(H)-dependent malate dehydrogenase (MDH) isoenzymes were detected in Phytomonas isolated from the lactiferous tubes of Euphorbia characias. The total specific activity in crude extracts using oxaloacetate as substrate was 3.3 U mg-1 of protein. The two isoenzymes had isoelectric points of 6.0 and 7.2, respectively. The acidic isoform represented 80% of the total activity in the cell and was present in the glycosome. It was purified to homogeneity by a method involving hydrophobic interaction chromatography on Phenyl-Sepharose followed by ionic exchange on CM-Sepharose and affinity chromatography on Blue-Sepharose. The purified glycosomal MDH is a homodimeric protein with a subunit molecular mass of 37 kDa and it has a low substrate specificity, since it was able to reduce both aromatic and aliphatic alpha-ketoacids as substrate including oxaloacetate, phenyl pyruvate, alpha-keto iso-caproate and pyruvate. The apparent K(m)s for oxaloacetate and NADH were 166 and 270 microM, respectively and for L-malate and NAD+, 3000 and 246 microM, respectively. The basic isoform was present in the mitochondrion. It has a high substrate specificity and an apparent K(m) of 132 and 63 microM for oxaloacetate and NADH, respectively, and of 450 and 91 microM, respectively, with L-malate and NAD+.

Alcohol Oxidoreductases↗

PubMed1997

Hydrolysis of esters by staphylococci.

The objective of this work was to characterize the hydrolysis of esters by staphylococci in order to understand if they could contribute to the release of free fatty acids in sausage. Cell-free extracts and extracellular concentrates of staphylococci were examined for esterase activities against p-nitrophenyl esters and for lipolytic activities against triolein. Staphylococci showed intracellular and extracellular esterase activities with different esterase electrophoretic patterns. Cell-free extracts of S. xylosus, S. warneri and S. saprophyticus preferentially hydrolysed p-nitrophenyl butyrate whereas their extracellular concentrates were mainly active against p-nitrophenyl butyrate, p-nitrophenyl caproate and p-nitrophenyl caprylate. In addition their extracellular concentrates hydrolysed triolein. The two strains of S. carnosus differed as they did not show pronounced p-nitrophenyl substrate specificity and did not hydrolyse triolein. Staphylococci hydrolysed esters at a high rate between 15 and 25 degrees C; acidic conditions inhibited the hydrolysis. The hydrolysis was also reduced when the water activity was decreased by addition of polyethylene glycol or glycerol.

Esterases↗