ACETYL ESTERASE IN BACILLUS CEREUS SPORES

1966 ◽  
Vol 44 (6) ◽  
pp. 671-675 ◽  
Author(s):  
Thomas L. Roberts ◽  
Harris Rosenkrantz
Keyword(s):  
Bacillus Cereus ◽  
Enzyme Inhibition ◽  
Esterase Activity ◽  
Fluorescein Diacetate ◽  
Bacterial Spores ◽  
Acetyl Esterase ◽  
Esterase Activities

The paucity of data on esterase activity in intact, dormant spores encouraged further examination of Bacillus cereus spores with more sensitive fluorescent methods. Esterase activities of intact and ballistically ruptured spore preparations against α-naphtyl acetate and fluorescein diacetate in phosphate and carbonate buffers were compared. Enzyme inhibition with toluene and molybdate was also inspected. It was found that intact spores and the supernatant from ruptured spores readily hydrolyzed both acetate substrates. Toluene caused approximately an 80% inhibition, whereas that with molybdate was complete. It was suggested that esterase activity in bacterial spores varies with species.

LIPASE AND ACETYL ESTERASE ACTIVITIES IN INTACT BACILLUS COAGULANS SPORES

1966 ◽  
Vol 44 (6) ◽  
pp. 677-685 ◽  
Author(s):  
Thomas L. Roberts ◽  
Harris Rosenkrantz
Keyword(s):  
Ethyl Acetate ◽  
Ultraviolet Light ◽  
Copper Acetate ◽  
Bacillus Coagulans ◽  
Fluorescein Diacetate ◽  
Ethyl Butyrate ◽  
Acetyl Esterase ◽  
Enzyme Substrates ◽  
Hydrolysis Of ◽  
Esterase Activities

Since data on esterase content of intact dormant spores are meager, a study was carried out with various enzyme substrates and several methods of product detection on intact and ruptured preparations of Bacillus coagulans. Measurement of hydrolysis of triacetin, naphthyl acetates, fluorescein diacetate, ethyl acetate, and ethyl butyrate demonstrated the presence of arylesterase, carboxylesterase, acetyl esterase, and lipase activities in both the intact and ruptured preparations of the non-germinated organism used. It was observed that spore esterase was inhibited by normal and basic copper acetate, eserine, taurocholate, 253.7 mμ ultraviolet light, and temperatures between 50 and 100 °C.

scholarly journals O-acetylated Gangliosides as Targets for Cancer Immunotherapy

Cells ◽  
2020 ◽  
Vol 9 (3) ◽  
pp. 741 ◽  
Author(s):  
Sumeyye Cavdarli ◽  
Philippe Delannoy ◽  
Sophie Groux-Degroote
Keyword(s):  
Cancer Immunotherapy ◽  
Current Knowledge ◽  
Cancer Development ◽  
Acetyl Esterase ◽  
Pathological Conditions ◽  
Ganglioside Biosynthesis ◽  
The Central Nervous System ◽  
Neuroectodermal Origin ◽  
Ganglioside Species ◽  
Esterase Activities

O-acetylation of sialic acid residues is one of the main modifications of gangliosides, and modulates ganglioside functions. O-acetylation of gangliosides is dependent on sialyl-O-acetyltransferases and sialyl-O-acetyl-esterase activities. CAS1 Domain-Containing Protein 1 (CASD1) is the only human sialyl-O-acetyltransferases (SOAT) described until now. O-acetylated ganglioside species are mainly expressed during embryonic development and in the central nervous system in healthy adults, but are re-expressed during cancer development and are considered as markers of cancers of neuroectodermal origin. However, the specific biological roles of O-acetylated gangliosides in developing and malignant tissues have not been extensively studied, mostly because of the requirement of specific approaches and tools for sample preparation and analysis. In this review, we summarize our current knowledge of ganglioside biosynthesis and expression in normal and pathological conditions, of ganglioside O-acetylation analysis and expression in cancers, and of the possible use of O-acetylated gangliosides as targets for cancer immunotherapy.

Metabolism of Ferulic Acid Sucrose Esters in Anthers of Tulipa cv. Apeldoorn: II. Highly Specific Degradation of the Esters by Different Esterase Activities

1988 ◽  
Vol 43 (9-10) ◽  
pp. 647-655 ◽  
Author(s):  
P. A. Bäumker ◽  
S. Arendt ◽  
R. Wiermann
Keyword(s):  
Ferulic Acid ◽  
Esterase Activity ◽  
Sinapic Acid ◽  
High Specificity ◽  
Degradation Process ◽  
Product Formation ◽  
Reversed Phase ◽  
Sucrose Esters ◽  
Degradation Reactions ◽  
Esterase Activities

Abstract Protein extracts from anthers of Tulipa cv. Apeldoorn catalyze the degradation of ferulic acid sucrose esters. Different products are generated when triferuloyl sucrose (TFS) and diferuloyl sucrose (DFS) were applied as substrates. By the aid of reversed-phase HPLC , TLC and spectroscopy the products could be identified as free ferulic acid, monoferuloyl sucrose ester [feruloylsucrose(mono)] and two different diesters of ferulic acid and sucrose [feruloylsucrose(di) and the endogenously occurring diferuloylsucrose (DFS)]. By means of protein fractionation (chromatofocusing, anion exchange HPLC and molecular sieving HPLC) , four different enzyme activities involved in the degradation process could be separated. According to their catalytic properties, they were characterized as esterases (= EA). The partially purified esterase activity I (EAI) obtained after fractionation by chromatofocusing catalyzes the formation of feruloylsucrose(di) and ferulic acid when TFS is used as substrate. Incubations with EA la or EA Ib isolated in smaller portions lead to the same product pattern. The esterase activity II (EA II) degrades TFS to ferulic acid and DFS . DFS as substrate is only accepted by the EA I activities, in all three cases ferulic acid and feruloyl sucrose(mono) are formed as products. The kinds of different degradation reactions clearly indicate that one enzyme (= the EA II activity) catalyzes exclusively the formation of DFS from TFS. Both enzymes, EA I and EA II, exhibit a high specificity towards ferulic acid sucrose esters. Hydroxycinnamic sucrose esters with only sinapic acid moieties do not function as substrates. When enzymatically formed sucrose esters like feruloylsucrose(di), feruloylsucrose(mono) and monosinapoylsucrose were used as substrates, no product formation could be observed. Applying SFS as substrate, only the ferulic acid moiety was released by EA I. Further, naturally occurring esters (glucose- and CoA-esters of p-coumaric, caffeic, ferulic and sinapic acid; chlorogenic acid; BGM ) tested so far were not degraded by EA I and EA II. It is assumed that these esterase activities play a specific role in the ferulic acid metabolism in Tulipa anthers.

Death rates of bacterial spores: nonlinear survivor curves

1975 ◽  
Vol 21 (10) ◽  
pp. 1464-1467 ◽  
Author(s):  
Youn W. Han
Keyword(s):  
Heat Resistance ◽  
Bacillus Cereus ◽  
Saline Solution ◽  
Physiological Saline ◽  
Bacterial Spores ◽  
Death Rates ◽  
Physiological Saline Solution ◽  
Spore Population

Nonlinear survivor curves were obtained when spores of Bacillus cereus were heated in physiological saline solution. Curvilinear survivor curves did not appear to be caused by experimental artifacts but by the heterogeneity of spore population with regard to heat resistance.

scholarly journals STUDIES OF ACID PHOSPHATASE AND NONSPECIFIC ESTERASE ACTIVITIES IN RAT ADRENAL GLANDS FOLLOWING OPERATIVE STRESS

1970 ◽  
Vol 18 (9) ◽  
pp. 650-659 ◽  
Author(s):  
S. R. CHOUDHURY ◽  
A. M. LUNDY
Keyword(s):  
Acid Phosphatase ◽  
Esterase Activity ◽  
Adrenal Glands ◽  
Surgical Stress ◽  
Cauda Equina ◽  
Hydrolytic Enzymes ◽  
Nonspecific Esterase ◽  
Starch Gel Electrophoresis ◽  
Operative Stress ◽  
Esterase Activities

Acid phosphatase and esterase activities were studied in adrenal glands obtained from rats killed at regular intervals following surgical stress (cauda equina transection). Zymograms of acid phosphatase produced by starch gel electrophoresis revealed increased reactivity in the operated samples. With esterases, a slightly different pattern was observed in the operated group, which exhibited a few additional bands particularly in the cathode region. This was confirmed by densitometric analysis of the gel strips. Two of these additional bands were organophosphate-sensitive and the remaining few were activated by p-chloromercuribenzoate. These latter bands appeared to arise from splitting of the preexisting organophosphate-resistant bands present in control zymograms. Biochemical assay of the two hydrolytic enzymes demonstrated a remarkable similarity in their responses to operative stress—probably implying a general lysosomal activation. Both enzymes exhibited a peak activity 8 hr after operation, followed by a gradual decline. Both organophosphate-sensitive and organophosphate-resistant esterases contributed toward the rise in total esterase activity. Histochemical studies on tissue sections revealed a more reactive adrenal cortex in the operated group, but were of little help in localizing the additional esterase activity observed in gel strips.

scholarly journals Characteristics and resistance to selected disinfectants of bacterial spores of Bacillus subtilis and Bacillus cereus

2018 ◽  
pp. 201-207
Author(s):  
Anna Kinga Kierzkowska
Keyword(s):  
Bacillus Subtilis ◽  
Bacillus Cereus ◽  
Pathogenic Bacteria ◽  
Bacterial Spores ◽  
Drug Resistant ◽  
Development Cycle

Despite the emergence of newer disinfectant preparations on the market, there are still no biocides that would effectively eliminate spores of multi-drug resistant pathogenic bacteria. For this reason, most commercially available sporicidal preparations are mixtures of several substances. The paper discusses the endospore characteristics, their development cycle and the list of currently effective substances used in mixtures of sporicidal preparations

scholarly journals Microwave assisted solvent-free mannich bases: synthesis, characterization and effects of these compounds on HCA I and HCA II isozymes

2021 ◽  
Vol 40 (1) ◽  
pp. 43
Author(s):  
Bülent Büyükkıdan ◽  
Nurgün Büyükkıdan ◽  
Metin Bülbül ◽  
Melek Yılmaz ◽  
Evren Derrun Arslanbay ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Esterase Activity ◽  
Inhibitory Concentration ◽  
Mannich Bases ◽  
Solvent Free ◽  
Inhibitory Effects ◽  
Solvent Free Conditions ◽  
Control Compound ◽  
Esterase Activities

Mannich bases (2a–d) of aromatic amines were synthesized by using a conventional microwave technique under solvent-free conditions and characterized by IR and NMR (1H and 13C) and elemental analysis. The inhibitory effects of the synthesized Mannich bases were examined in vitro by using hydratase and esterase assays on carbonic anhydrase I and II isozymes (hCA, EC 4.2.1.1) purified from human erythrocyte cells. Acetazolamide was used as the control compound. The values of IC50, the half-maximum inhibitory concentration, were found for hydratase and esterase activities. Only two compounds (2b and 2d) exhibited poor hCA I and hCA II inhibition effects on esterase activity. In contrast, compounds 2a and 2c could be used as carbonic anhydrase activators as a result of the increased esterase activity of hCA I and hCA II isozymes.

Studies on the Enzymatic Activity of the Antihemophilic Factor (Factor VIII)

1967 ◽  
Vol 17 (01/02) ◽  
pp. 188-193 ◽  
Author(s):  
S van Creveld ◽  
I. A Mochtar ◽  
C. N Pascha
Keyword(s):  
Enzymatic Activity ◽  
Factor Viii ◽  
Esterase Activity ◽  
Barium Sulphate ◽  
Screening Tests ◽  
Normal Human ◽  
The Stability ◽  
Fraction I ◽  
Antihemophilic Factor ◽  
Esterase Activities

SummaryPreparations of normal human antihemophilic factor (AHF, factor VIII) obtained by continuous free electrophoresis in the “Elphor” apparatus, were investigated for enzymatic activity on various substrates. A number of enzymatic activities could be excluded by screening tests, performed with fraction I of Cohn. In some preparations esterase-activity was demonstrable on the substrates benzoyl-arginyl-ethylester (BAEE) and on glycerol tributyrate. There was, however, no correlation between these esterase-activities and the AHF-activity in the preparations. Moreover, the stability of the esterase at 4° C was much greater than the stability of the AHF-activity. We therefore assume that the AHF has no enzymatic activity on these substrates under the conditions of the tests. Attempts to activate AHF by calcium, magnesium or serum, were unsuccessful. Both esterase-activities were also present in fraction I of Cohn prepared from normal human citrated or resin plasma. The esterase-activity on BAEE is removed from resin plasma by adsorption to barium sulphate. The esterase-activity on glycerol tributyrate is not adsorbed.

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