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Artykuły w czasopismach na temat „4-methylumbelliferyl substrates”

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Data publikacji: 3 czerwca 2025

Data aktualizacji: 31 lipca 2025

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1

Garcia-Sastre, A., E. Villar, J. C. Manuguerra, C. Hannoun, and J. A. Cabezas. "Activity of influenza C virus O-acetylesterase with O-acetyl-containing compounds." Biochemical Journal 273, no. 2 (1991): 435–41. http://dx.doi.org/10.1042/bj2730435.

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Influenza C virus (strain C/Johannesburg/1/66) was grown, harvested, purified and used as source for the enzyme O-acetylesterase (N-acyl-O-acetylneuraminate O-acetylhydrolase; EC 3.1.1.53). This activity was studied and characterized with regard to some new substrates. The pH optimum of the enzyme is around 7.6, its stability at different pH values shows a result similar to that of the pH optimum, and its activity is well maintained in the pH range from 7.0 to 8.5 (all these tests were performed with 4-nitrophenyl acetate as substrate). Remarkable differences were found in the values of both K

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2

Bhat, K. M., A. J. Hay, M. Claeyssens та T. M. Wood. "Study of the mode of action and site-specificity of the endo-(1→4)-β-d-glucanases of the fungus Penicillium pinophilum with normal, 1-3H-labelled, reduced and chromogenic cello-oligosaccharides". Biochemical Journal 266, № 2 (1990): 371–78. http://dx.doi.org/10.1042/bj2660371.

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The modes of action of the five major endo-(1→4)-beta-D-glucanases (I, II, III, IV and V) purified from Penicillium pinophilum cellulase were compared by h.p.l.c. analysis, with normal, 1-3H-labelled and reduced cello-oligosaccharides and 4-methylumbelliferyl glycosides as substrates. Significant differences were observed in the preferred site of cleavage even when substrates with the same number of glycosidic bonds were compared. Thus, although endoglucanase I was unable to attack normal cello-oligosaccharides shorter than degree of polymerization 6, it hydrolysed reduced cellopentaose to yie

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3

Barth, M. G. M., and P. D. Bridge. "4-Methylumbelliferyl substituted compounds as fluorogenic substrates for fungal extracellular enzymes." Letters in Applied Microbiology 9, no. 5 (1989): 177–79. http://dx.doi.org/10.1111/j.1472-765x.1989.tb00318.x.

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4

Miller, Morten, Ansa Palojärvi, Andrea Rangger, Morten Reeslev, and Annelise Kjøller. "The Use of Fluorogenic Substrates To Measure Fungal Presence and Activity in Soil." Applied and Environmental Microbiology 64, no. 2 (1998): 613–17. http://dx.doi.org/10.1128/aem.64.2.613-617.1998.

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ABSTRACT Our objective was to determine if 4-methylumbelliferyl-labelled enzyme substrates could be used to detect and quantify specific components of chitinase and cellulase activities as specific indicators of the presence and activity of fungal biomass. The fluorogenic substrates 4-methylumbelliferyl (MUF)N-acetyl-β-d-glucosaminide and MUF β-d-lactoside were used for the detection and quantification of β-N-acetylglucosaminidase (EC 3.2.1.30 ) (NAGase) and endo 1,4-β-glucanase (EC 3.2.1.4 )/cellobiohydrolase (EC3.2.1.91 ) (CELase), respectively. Culture screenings on solid media showed a wid

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5

Adcock, Philip W., and Christopher P. Saint. "Rapid Confirmation of Clostridium perfringens by Using Chromogenic and Fluorogenic Substrates." Applied and Environmental Microbiology 67, no. 9 (2001): 4382–84. http://dx.doi.org/10.1128/aem.67.9.4382-4384.2001.

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ABSTRACT The use of 4-methylumbelliferyl phosphate (MUP) andortho-nitrophenyl-β-d-galactopyranoside (ONPG) for the identification of Clostridium perfringenswas investigated. A liquid assay containing both MUP and ONPG was a highly specific alternative method for C. perfringensconfirmation, reducing incubation time from 48 to only 4 h. The assay solution is easy to prepare, does not require anaerobic conditions for use, and has an extended shelf life.

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6

Fiksdal, L., I. Tryland, and H. Nelis. "Rapid detection of coliform bacteria and influence of non-target bacteria." Water Science and Technology 35, no. 11-12 (1997): 415–18. http://dx.doi.org/10.2166/wst.1997.0769.

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Enzymatic hydrolysis of fluorogenic substrates (4-methylumbelliferyl-β-D-galactoside, 4-methylumbelliferyl-β-D-glucuronide) has been used for rapid (25min) detection of indicators of faecal water pollution, i.e. coliform and thermotolerant coliform bacteria. In the present work, enzymatic activities and different groups of bacteria (i.e. thermotolerant coliforms, coliforms, β-galactosidase positive and β-glucuronidase positive bacteria) from sewage effluent and polluted river water have been investigated. Ratios of the order of 1:10 between coliforms and β-galactosidase positive bacteria were

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7

Bussink, Anton P., Marri Verhoek, Jocelyne Vreede, et al. "Common G102S polymorphism in chitotriosidase differentially affects activity towards 4-methylumbelliferyl substrates." FEBS Journal 276, no. 19 (2009): 5678–88. http://dx.doi.org/10.1111/j.1742-4658.2009.07259.x.

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8

Luyten, G. P., A. T. Hoogeveen, and H. Galjaard. "A fluorescence staining method for the demonstration and measurement of lysosomal enzyme activities in single cells." Journal of Histochemistry & Cytochemistry 33, no. 9 (1985): 965–68. http://dx.doi.org/10.1177/33.9.3926869.

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A cytochemical fluorescence method is described that makes possible simple, rapid, and specific demonstration and measurement of the activities of a wide variety of lysosomal enzymes in single cells using 4-methylumbelliferyl derivatives as substrates. The validity of the method and a number of applications using normal and mutant human cells are presented.

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9

Thompson, Hayley, Karen A. Homer, Susmitha Rao, Veronica Booth, and Arthur H. F. Hosie. "An Orthologue of Bacteroides fragilis NanH Is the Principal Sialidase in Tannerella forsythia." Journal of Bacteriology 191, no. 11 (2009): 3623–28. http://dx.doi.org/10.1128/jb.01618-08.

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ABSTRACT Sialidase activity is a putative virulence factor of the anaerobic periodontal pathogen Tannerella forsythia, but it is uncertain which genes encode this activity. Characterization of a putative sialidase, SiaHI, by others, indicated that this protein alone may not be responsible for all of the sialidase activity. We describe a second sialidase in T. forsythia (TF0035), an orthologue of Bacteroides fragilis NanH, and its expression in Escherichia coli. Sialidase activity of the expressed NanH was confirmed by using 2′-(4-methylumbelliferyl)-α-d-N-acetylneuraminic acid as a substrate.

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10

Kämpfer, Peter, Richard Keuch, and Wolfgang Dott. "Glycosidase profiles of Bacillus spp. and their value for species differentiation." Canadian Journal of Microbiology 39, no. 8 (1993): 808–11. http://dx.doi.org/10.1139/m93-119.

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A total of 268 strains of Bacillus spp. were investigated for their ability to hydrolyze 14 different fluorogenic 4-methylumbelliferyl-linked glycosidase substrates within 6 and 24 h of incubation. Glycosidase profiles were heterogeneous within the genus and some of the tests showed high separation index values; the profiles can therefore improve the differentiation of Bacillus spp. However, glycosidase profiles are not sufficient for unambiguous identification and should be used in combination with other biochemical tests.Key words: Bacillus, glycosidases, fluorogenic substrates, differentiat

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11

DURANT, PAMELA J., MARILYN S. BARTLETT, MARGARET M. SHAW, SHERRY F. QUEENER, and JAMES W. SMITH. "Demonstration of Esterase Activity in Pneumocystis carinii by Cleavage of 4-Methylumbelliferyl Substrates." Journal of Eukaryotic Microbiology 43, no. 5 (1996): 45S. http://dx.doi.org/10.1111/j.1550-7408.1996.tb04981.x.

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12

Klausegger, Alfred, Birgit Strobl, Gerhard Regl, Alexandra Kaser, Willem Luytjes, and Reinhard Vlasak. "Identification of a Coronavirus Hemagglutinin-Esterase with a Substrate Specificity Different from Those of Influenza C Virus and Bovine Coronavirus." Journal of Virology 73, no. 5 (1999): 3737–43. http://dx.doi.org/10.1128/jvi.73.5.3737-3743.1999.

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ABSTRACT We have characterized the hemagglutinin-esterase (HE) of puffinosis virus (PV), a coronavirus closely related to mouse hepatitis virus (MHV). Analysis of the cloned gene revealed approximately 85% sequence identity to HE proteins of MHV and approximately 60% identity to the corresponding esterase of bovine coronavirus. The HE protein exhibited acetylesterase activity with synthetic substratesp-nitrophenyl acetate, α-naphthyl acetate, and 4-methylumbelliferyl acetate. In contrast to other viral esterases, no activity was detectable with natural substrates containing 9-O-acetylated sial

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13

Graf, Felix Marcel Rainer, та Markus Buchhaupt. "Comparative Investigations on Different β-Glucosidase Surrogate Substrates". Fermentation 8, № 2 (2022): 83. http://dx.doi.org/10.3390/fermentation8020083.

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β-glucosidases are hydrolyzing enzymes which can release many aroma-active compounds from their glycoside form. Several yeasts produce these enzymes and thus are applied during the wine production process. To be able to test specific organisms for the presence of β-glucosidases and to investigate this enzyme activity, four main surrogate substrates have been described. The properties and applicability of these compounds, named arbutin (hydroquinone-β-D-glucopyranoside), esculin (6-O-(-D-glucosyl)aesculetin), 4-nitrophenyl-β-D-glucopyranoside (pNPG) and 4-methylumbelliferyl-β-D-glucopyranoside

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14

Spaltro, J., and J. A. Alhadeff. "Cellular localization and substrate specificity of isoelectric forms of human liver neuraminidase activity." Biochemical Journal 241, no. 1 (1987): 137–43. http://dx.doi.org/10.1042/bj2410137.

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The four major isoelectric forms of human liver neuraminidase (with pI values between 3.4 and 4.8) have been isolated by preparative isoelectric focusing and characterized with regard to their substrate specificity using glycoprotein, glycopeptide, oligosaccharide and ganglioside natural substrates. All forms exhibited a rather broad linkage specificity and were capable of hydrolyzing sialic acid glycosidically linked alpha 2-3, alpha 2-6 and alpha 2-8, although differential rates of hydrolysis of the substrates were found for each form. The most acidic form 1 (pI 3.4) was most active on sialy

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15

Wang, L. X., N. O. Keyhani, S. Roseman, and Y. C. Lee. "4-Methylumbelliferyl glycosides of N-acetyl 4-thiochito-oligosaccharides as fluorogenic substrates for chitodextrinase from Vibrio furnissii." Glycobiology 7, no. 6 (1997): 855–60. http://dx.doi.org/10.1093/glycob/7.6.855.

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16

ABEL, Mireia, Karin IVERSEN, Antoni PLANAS, and Ulla CHRISTENSEN. "Pre-steady-state kinetics of Bacillus licheniformis 1,3-1,4-beta-glucanase: evidence for a regulatory binding site." Biochemical Journal 371, no. 3 (2003): 997–1003. http://dx.doi.org/10.1042/bj20021504.

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In a previous paper, we reported the first stopped-flow experiments on a Bacillus licheniformis 1,3-1,4-β-glucanase [Abel, Planas and Christensen (2001) Biochem. J. 357, 195–202]. It was shown that the pre-steady-state kinetics of the 1,3-1,4-β-glucanase using the substrate 4-methylumbelliferyl 3-O-β-cellobiosyl-β-d-glucoside may be explained by a reaction scheme involving an induced fit and the binding of two substrates as well as a second enzymic conformational change, whereas the results definitely could not be explained in terms of the simple double-displacement scheme. In the present stud

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17

Gold, Henrik, Stefan Munneke, Jasper Dinkelaar, et al. "A practical synthesis of capped 4-methylumbelliferyl hyaluronan disaccharides and tetrasaccharides as potential hyaluronidase substrates." Carbohydrate Research 346, no. 12 (2011): 1467–78. http://dx.doi.org/10.1016/j.carres.2011.03.042.

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18

Han, G. Y., X. H. Fan, X. B. Jin, and D. P. Wang. "Specific Detection and Properties of Enzyme Hydrolyzing Phosphonate Ester in Serum." Clinical Chemistry 38, no. 3 (1992): 377–80. http://dx.doi.org/10.1093/clinchem/38.3.377.

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Abstract An enzyme capable of hydrolyzing 4-methylumbelliferyl phenylphosphonate to 4-methylumbelliferone and phenylphosphonic acid has been detected in human serum. It has a Km value of 1.72 x 10(-4) mol/L, has an optimum pH of 8.8-9.1 in Tris buffer, and shows maximum activity at 60 degrees C (30 min). The enzymic activity can be inhibited by Na3PO4, EDTA, and cysteine. We saw no effect of CuSO4, adenosine, thymidine, NaN3, diethyl p-nitrophenyl phosphate, p-chloromercuribenzoate, isopropyl fluorophosphate, or eserine on the enzymic activity. The enzyme cannot hydrolyze substrates of phospho

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19

Münster, U., P. Einiö, and J. Nurminen. "Evaluation of the measurements of extracellular enzyme activities in a polyhumic lake by means of studies with 4-methylumbelliferyl-substrates." Archiv für Hydrobiologie 115, no. 3 (1989): 321–37. http://dx.doi.org/10.1127/archiv-hydrobiol/115/1989/321.

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20

Eneyskaya, Elena V., Dina R. Ivanen, Konstantin A. Shabalin та ін. "Chemo-enzymatic synthesis of 4-methylumbelliferyl β-(1→4)-d-xylooligosides: new substrates for β-d-xylanase assays". Org. Biomol. Chem. 3, № 1 (2005): 146–51. http://dx.doi.org/10.1039/b409583a.

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21

Dahbi, Samir, Jean-Claude Jacquinet, Isabelle Bertin-Jung та ін. "Synthesis of a library of variously modified 4-methylumbelliferyl xylosides and a structure–activity study of human β4GalT7". Organic & Biomolecular Chemistry 15, № 45 (2017): 9653–69. http://dx.doi.org/10.1039/c7ob02530k.

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22

Park, Jun-Young, Jisu Ha, Yoonseok Choi, Pahn-Shick Chang, and Kyung-Min Park. "Optimization of Spectrophotometric and Fluorometric Assays Using Alternative Substrates for the High-Throughput Screening of Lipase Activity." Journal of Chemistry 2021 (July 27, 2021): 1–10. http://dx.doi.org/10.1155/2021/3688124.

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The effects of reaction conditions on the spectrophotometric and fluorometric assays using alternative substrates (p-nitrophenyl palmitate and 4-methylumbelliferyl oleate) were investigated to optimize them for the high-throughput screening of lipase activity from agricultural products. Four model lipases from Chromobacterium viscosum, Pseudomonas fluorescens, Sus scrofa pancreas, and wheat germ (Triticum aestivum) were allowed to hydrolyze the alternative substrates at different substrate concentrations (1–5 mM), operating pH (5.0–8.0), and operating temperatures (25–55°C). The results show t

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23

Ondrejková, Ema, Helena Hronská, Vladimír Štefuca, Mária Bláhová та Michal Rosenberg. "Isolation, Specificity, and Application of β-N-Acetylhexosaminidases from Penicillium crustosum". Applied Sciences 13, № 6 (2023): 3399. http://dx.doi.org/10.3390/app13063399.

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β-N-acetylhexosaminidases have great potential in applied biocatalysis owing to their ability to act on a wide range of natural and modified substrates. In this work, β-N-acetylhexosaminidases from four Penicillium crustosum strains (PcHex) were studied. The production strains showed the highest enzymatic activity in the culture medium after 11–14 days of cultivation. The specific activity of the isolated and purified PcHex of hydrolysis of 4-nitrophenyl-N-acetyl-β-D-galactopyranoside was 15–20 U/mg protein. All isolated β-N-acetylhexosaminidases showed similar pH–activity profiles, with the o

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24

HUMBERT, GERARD, MARIE-FRANCE GUINGAMP, and GUY LINDEN. "Method for the measurement of lipase activity in milk." Journal of Dairy Research 64, no. 3 (1997): 465–69. http://dx.doi.org/10.1017/s0022029997002288.

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Lipolysis has many effects in dairy technology. Undesirable consequences include deleterious effects on the organoleptic properties of milk and some cheeses; however, it is desirable in some other cheeses.The usual methods for detecting lipolysis in milk measure the amounts of free fatty acids liberated from triacylglycerols (International Dairy Federation, 1991). Lipase activity is detected by incubation of samples with substrates such as tributyrin (Castberg et al. 1975) or triolein (Nilsson-Ehle & Schotz, 1976; Shirai et al. 1982). A few reports describe methods using synthetic chromoge

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25

KLEINEIDAM, Reinhard G., Kimio FURUHATA, Haruo OGURA та Roland SCHAUER. "4-Methylumbelliferyl-α-Glycosides of Partially0-AcetylatedN-Acetylneuraminic Acids as Substrates of Bacterial and Viral Sialidases". Biological Chemistry Hoppe-Seyler 371, № 2 (1990): 715–20. http://dx.doi.org/10.1515/bchm3.1990.371.2.715.

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26

WATANABE, Takeshi, Yumiko ARIGA, Urara SATO, et al. "Aromatic residues within the substrate-binding cleft of Bacillus circulans chitinase A1 are essential for hydrolysis of crystalline chitin." Biochemical Journal 376, no. 1 (2003): 237–44. http://dx.doi.org/10.1042/bj20030419.

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Bacillus circulans chitinase A1 (ChiA1) has a deep substrate-binding cleft on top of its (β/α)8-barrel catalytic domain and an interaction between the aromatic residues in this cleft and bound oligosaccharide has been suggested. To study the roles of these aromatic residues, especially in crystalline-chitin hydrolysis, site-directed mutagenesis of these residues was carried out. Y56A and W53A mutations at subsites −5 and −3, respectively, selectively decreased the hydrolysing activity against highly crystalline β-chitin. W164A and W285A mutations at subsites +1 and +2, respectively, decreased

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27

Freeman, C., та J. J. Hopwood. "Human α-l-iduronidase. Catalytic properties and an integrated role in the lysosomal degradation of heparan sulphate". Biochemical Journal 282, № 3 (1992): 899–908. http://dx.doi.org/10.1042/bj2820899.

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The kinetic parameters (Km and kcat) of human liver alpha-L-iduronidase were determined with a variety of heparin-derived disaccharide and tetrasaccharide substrates. More structurally complex substrates, in which several aspects of the aglycone structure of the natural substrates heparin and heparan sulphate were maintained, were hydrolysed with catalytic efficiencies up to 255 times that observed for the simplest disaccharide substrate to be hydrolysed. The major aglycone structure that influenced both substrate binding and enzyme activity was the presence of a C-6 sulphate ester on the resi

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28

Pantoja, S., M. H. Gutiérrez, P. Ampuero, and E. Tejos. "Degradation capability of the coastal environment adjacent to the Itata River in central Chile (36.5° S)." Biogeosciences 8, no. 8 (2011): 2063–74. http://dx.doi.org/10.5194/bg-8-2063-2011.

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Abstract. The response of the coastal ocean influenced by both river discharges and inputs of photosynthetically derived organic carbon product of upwelling, was evaluated by estimating rates of microbial hydrolysis of macromolecules with the goal of estimating the potential degradation capability of the coastal ecosystem off central Chile. Extracellular enzymatic activity (EEA) in seawater was dominated by aminopeptidase activity on substrate L-leucine-4-methyl-7-coumarinylamide (MCA-leu) (1.2 to 182 nmol l−1 h−1) followed by 4-methylumbelliferyl-ß-D-glucoside (MUF-glu) (0.08–61 nmol l−1 h−1)

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29

Malet, Carles, Josep Lluis Viladot, Ana Ochoa, Belen Gallégo, Carme Brosa та Antoni Planas. "Synthesis of 4-methylumbelliferyl-β-d-glucan oligosaccharides as specific chromophoric substrates of (1 → 3),(1 → 4)-β-d-glucan 4-glucanohydrolases". Carbohydrate Research 274 (вересень 1995): 285–301. http://dx.doi.org/10.1016/0008-6215(95)00102-y.

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30

Kawano, J., and E. Aikawa. "Ultrastructural localization of arylsulfatase C activity in rat kidney." Journal of Histochemistry & Cytochemistry 35, no. 5 (1987): 523–30. http://dx.doi.org/10.1177/35.5.3470383.

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Metal precipitation techniques for ultrastructural demonstration of arylsulfatase C activity were studied in rat kidney. Possible substrates for the techniques were biochemically tested with regard to their velocity of enzymatic hydrolysis and their specificity for arylsulfatase C. Effects of buffers and capturing metals were also examined. The results of these biochemical studies were then verified histochemically. Incubation in a medium containing 1 mM 4-methylumbelliferyl sulfate, 1% barium chloride, 0.1 M imidazole-HCl buffer (pH 7.5), and 5% sucrose achieved identifiable results in adequa

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31

Honda, Yuji, Shinji Tanimori, Mitsunori Kirihata, et al. "Chemo- and enzymatic synthesis of partially and fully N -deacetylated 4-methylumbelliferyl chitobiosides: Fluorogenic substrates for chitinase." Bioorganic & Medicinal Chemistry Letters 10, no. 8 (2000): 827–29. http://dx.doi.org/10.1016/s0960-894x(00)00116-5.

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32

Gibson, G. J., G. T. Saccone, D. A. Brooks, P. R. Clements, and J. J. Hopwood. "Human N-acetylgalactosamine-4-sulphate sulphatase. Purification, monoclonal antibody production and native and subunit Mr values." Biochemical Journal 248, no. 3 (1987): 755–64. http://dx.doi.org/10.1042/bj2480755.

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Initial purification of N-acetylgalactosamine-4-sulphate sulphatase from human liver homogenates containing approx. 1 mg of enzyme in 26 g of soluble proteins was achieved by a six-column chromatography procedure and yielded approx. 40 micrograms of a single major protein species. Enzyme thus prepared was used to produce N-acetylgalactosamine-4-sulphate sulphatase-specific monoclonal antibodies. The use of a monoclonal antibody linked to a solid support facilitated the purification of approx. 0.5 mg of N-acetylgalactosamine-4-sulphate sulphatase from a similar liver homogenate. Moreover the en

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33

Bielicki, J., and J. J. Hopwood. "Human liver N-acetylgalactosamine 6-sulphatase. Purification and characterization." Biochemical Journal 279, no. 2 (1991): 515–20. http://dx.doi.org/10.1042/bj2790515.

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Human N-acetylgalactosamine 6-sulphatase (EC 3.1.6.14), which is involved in the lysosomal degradation of the glycosaminoglycans keratan sulphate and chondroitin 6-sulphate, was purified more than 130,000-fold in 2.8% yield from liver by an eight-step column procedure. One major form was identified with a pI of 5.7 and a native molecular mass of 62 kDa by gel filtration. When analysed by SDS/PAGE, dithioerythritol-reduced enzyme contained polypeptides of molecular masses 57 kDa, 39 kDa and 19 kDa, whereas non-reduced enzyme contained a major polypeptide of molecular mass 70 kDa. It is proposed

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34

Bauters, T. G., R. Peleman, M. Moerman, et al. "Membrane Filtration Test for Rapid Presumptive Differentiation of Four Candida Species." Journal of Clinical Microbiology 37, no. 5 (1999): 1498–502. http://dx.doi.org/10.1128/jcm.37.5.1498-1502.1999.

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A rapid enzymatic two-step test for the presumptive differentiation of four Candida species commonly occurring in various clinical samples is described. The technique involves membrane filtration of a liquid sample, followed by preincubation of the membrane filter on Sabouraud glucose agar supplemented with ticarcillin-clavulanic acid to yield microcolonies. In a separate assay step, parts of the filter are placed on absorbent pads impregnated with fluorogenic 4-methylumbelliferyl (4-MU) enzyme substrates (4-MU-N-acetyl-β-d-galactosaminide, 4-MU-phosphate, 4-MU-pyrophosphate, and 4-MU-β-d-gala

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35

Wurzer, Walter Juergen, Karola Obojes, and Reinhard Vlasak. "The sialate-4-O-acetylesterases of coronaviruses related to mouse hepatitis virus: a proposal to reorganize group 2 Coronaviridae." Journal of General Virology 83, no. 2 (2002): 395–402. http://dx.doi.org/10.1099/0022-1317-83-2-395.

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Group 2 coronaviruses are characterized within the order Nidovirales by a unique genome organization. A characteristic feature of group 2 coronaviruses is the presence of a gene encoding the haemagglutinin–esterase (HE) protein, which is absent in coronaviruses of groups 1 and 3. At least three coronavirus strains within group 2 expressed a structural protein with sialate-4-O-acetylesterase activity, distinguishing them from other members of group 2, which encode an enzyme specific for 5-N-acetyl-9-O-acetylneuraminic acid. The esterases of mouse hepatitis virus (MHV) strains S and JHM and puff

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Borriss, Rainer, Martin Krah, Harry Brumer та ін. "Enzymatic synthesis of 4-methylumbelliferyl (1→3)-β-d-glucooligosaccharides—new substrates for β-1,3-1,4-d-glucanase". Carbohydrate Research 338, № 14 (2003): 1455–67. http://dx.doi.org/10.1016/s0008-6215(03)00199-x.

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Tryland, I., та L. Fiksdal. "Enzyme Characteristics of β-d-Galactosidase- and β-d-Glucuronidase-Positive Bacteria and Their Interference in Rapid Methods for Detection of Waterborne Coliforms andEscherichia coli". Applied and Environmental Microbiology 64, № 3 (1998): 1018–23. http://dx.doi.org/10.1128/aem.64.3.1018-1023.1998.

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ABSTRACT Bacteria which were β-d-galactosidase and β-d-glucuronidase positive or expressed only one of these enzymes were isolated from environmental water samples. The enzymatic activity of these bacteria was measured in 25-min assays by using the fluorogenic substrates 4-methylumbelliferyl-β-d-galactoside and 4-methylumbelliferyl-β-d-glucuronide. The enzyme activity, enzyme induction, and enzyme temperature characteristics of target and nontarget bacteria in assays aimed at detecting coliform bacteria and Escherichia coli were investigated. The potential interference of false-positive bacter

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MARTINS, E., and E. P. B. CONTEL. "African dung beetle Onthophagus gazella Fabricius (Coleoptera: Scarabaeidae) esterase isozymes." Brazilian Journal of Biology 61, no. 4 (2001): 645–50. http://dx.doi.org/10.1590/s1519-69842001000400014.

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African beetles Onthophagus gazella from both sexes were analyzed by electrophoresis for an investigation of esterase isozymes using alpha-naphthyl propionate and methylumbelliferyl propionate as substrates. Only one of the esterases (Est. 6) reacted with one of the substrates (alpha-naphthyl propionate). Six areas of activity were found, two of them being polymorphic (Est. 3 and Est. 4). For presence of Est. 3, 337 individuals were analyzed, including descendants of 32 controlled crossings: two alleles were identified, whose frequencies are Est. 3A = 0.447 and Est. 3B = 0.553. The population

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Skudlarek, M. D., D. R. P. Tulsiani та M. C. Orgebin-Crist. "Rat epididymal luminal fluid acid β-d-galactosidase optimally hydrolyses glycoprotein substrate at neutral pH". Biochemical Journal 286, № 3 (1992): 907–14. http://dx.doi.org/10.1042/bj2860907.

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Several glycosidases, purified and characterized from mammalian tissues, have been shown to be optimally active under acidic conditions when p-nitrophenyl (PNP) or 4-methylumbelliferyl glycosides are used as substrates. Although high levels of the glycosidases are present in the epididymal lumen, their physiological role remains uncertain. To be functional, the glycosidases are expected to be enzymatically active at or near the physiological pH of luminal fluid. In this report, we demonstrate that the rat epididymal luminal fluid beta-D-galactosidase, optimally active toward PNP beta-D-galacto

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He, Xingxuan, and Edward H. Schuchman. "Identification of a Novel Acid Sphingomyelinase Activity Associated with Recombinant Human Acid Ceramidase." Biomolecules 13, no. 11 (2023): 1623. http://dx.doi.org/10.3390/biom13111623.

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Acid ceramidase (AC) is a lysosomal enzyme required to hydrolyze ceramide to sphingosine by the removal of the fatty acid moiety. An inherited deficiency in this activity results in two disorders, Farber Lipogranulomatosis and spinal muscular atrophy with myoclonic epilepsy, leading to the accumulation of ceramides and other sphingolipids in various cells and tissues. In addition to ceramide hydrolysis, several other activities have been attributed to AC, including a reverse reaction that synthesizes ceramide from free fatty acids and sphingosine, and a deacylase activity that removes fatty ac

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Sohaskey, Charles D., and Alan G. Barbour. "Spirochaeta aurantia Has Diacetyl Chloramphenicol Esterase Activity." Journal of Bacteriology 182, no. 7 (2000): 1930–34. http://dx.doi.org/10.1128/jb.182.7.1930-1934.2000.

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ABSTRACT The free-living spirochete Spirochaeta aurantia was nearly as susceptible to diacetyl chloramphenicol, the product of chloramphenicol acetyltransferase, as it was to chloramphenicol itself. This unexpected susceptibility to diacetyl chloramphenicol was wholly or partly the consequence of intrinsic carboxylesterase activity, as indicated by high-performance liquid chromatography, thin-layer chromatography, and microbiological assays. The esterase converted the diacetate to chloramphenicol, thus inhibiting spirochete growth. The esterase activity was cell associated, reduced by proteina

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Waters, P. J., A. P. Corfield, R. Eisenthal, and C. A. Pennock. "Freeze-stable sialidase activity in human leucocytes: substrate specificity, inhibitor susceptibility, detergent requirements and subcellular localization." Biochemical Journal 301, no. 3 (1994): 777–84. http://dx.doi.org/10.1042/bj3010777.

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Human leucocytes contain a freeze-stable sialidase (neuraminidase; EC 3.2.1.18) activity in addition to the better-characterized lysosomal freeze-labile enzyme. In order to discriminate between the sialidase activities detected with the synthetic fluorimetric substrate 4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid (MU-Neu5Ac), different tritiated sialoglycoconjugate substrates were prepared. Using this sensitive radioactive assay system, leucocyte sialidase activity towards glycoproteins was shown to be labile to repeated freeze-thawing, but a Triton-stimulated activity towards ganglios

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Shipkowski, Stephanie, та Jean E. Brenchley. "Characterization of an Unusual Cold-Active β-Glucosidase Belonging to Family 3 of the Glycoside Hydrolases from the Psychrophilic Isolate Paenibacillus sp. Strain C7". Applied and Environmental Microbiology 71, № 8 (2005): 4225–32. http://dx.doi.org/10.1128/aem.71.8.4225-4232.2005.

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ABSTRACT We selected for spore-forming psychrophilic bacteria able to use lactose as a carbon source and one isolate, designated Paenibacillus sp. strain C7, that was phylogenetically related to, but distinct from both Paenibacillus macquariensis and Paenibacillus antarcticus. Some Escherichia coli transformants obtained with genomic DNA from this isolate hydrolyzed X-Gal (5-bromo-4-chloro-3-indoyl-β-d-galactopyranoside) only below 30°C, an indication of cold-active β-galactosidase activity. Sequencing of the cloned insert revealed an open reading frame encoding a 756-amino acid protein that,

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P., W. H. K. P. Daulagala. "Induction and Expression of Chitinases from Four Sub Species of Bacillus thuringiensis." Journal of Advances in Microbiology 3, no. 1 (2017): 1–8. https://doi.org/10.9734/JAMB/2017/34084.

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Chitin is a naturally occurring linear polymer of <em>N</em>-acetylglucosamine and the major structural component of fungal cell walls and exoskeletons of insects and arthropods. Chitinases are the enzymes that breakdown chitin to economically important derivatives and found in a range of organisms including bacteria, insects, crustaceans, invertebrates, some vertebrates and higher plants. In the present study, four <em>Bacillus thuringiensis </em>(<em>Bt</em>)<em> </em>isolates were grown in media supplemented with 0.1% (w/v) regenerated chitin and chitinase inducing medium and screened for c

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Hall, J., S. Ali, M. Azim Surani, et al. "The generation of non-ruminant transgenic animals with cellulolytic capacity." Proceedings of the British Society of Animal Production (1972) 1993 (March 1993): 153. http://dx.doi.org/10.1017/s0308229600024776.

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In non-ruminant livestock the energy which can be derived from dietary cellulose and xylan is limited by the inefficient microbial fermentation of these polymers in the hind-gut. Furthermore, in poultry, cereal-derived plant structural polysaccharides impair normal digestive function through the formation of gel-like structures that trap nutrients which are therefore unavailable to the animal. The nutrition of non-ruminant livestock could be significantly improved by the depolymerization of plant structural polysaccharides, through the introduction of cellulase activity in the small intestines

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Reilly, Thomas J., Deborah L. Chance, Michael J. Calcutt, et al. "Characterization of a Unique Class C Acid Phosphatase from Clostridium perfringens." Applied and Environmental Microbiology 75, no. 11 (2009): 3745–54. http://dx.doi.org/10.1128/aem.01599-08.

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ABSTRACT Clostridium perfringens is a gram-positive anaerobe and a pathogen of medical importance. The detection of acid phosphatase activity is a powerful diagnostic indicator of the presence of C. perfringens among anaerobic isolates; however, characterization of the enzyme has not previously been reported. Provided here are details of the characterization of a soluble recombinant form of this cell-associated enzyme. The denatured enzyme was ∼31 kDa and a homodimer in solution. It catalyzed the hydrolysis of several substrates, including para-nitrophenyl phosphate, 4-methylumbelliferyl phosp

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Honda, Yuji, Shinji Tanimori, Mitsunori Kirihata, et al. "Kinetic analysis of the reaction catalyzed by chitinase A1 from Bacillus circulans WL-12 toward the novel substrates, partially N -deacetylated 4-methylumbelliferyl chitobiosides." FEBS Letters 476, no. 3 (2000): 194–97. http://dx.doi.org/10.1016/s0014-5793(00)01729-4.

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Kumar, Arun Babu, Sophia Masi, Farideh Ghomashchi, et al. "Tandem Mass Spectrometry Has a Larger Analytical Range than Fluorescence Assays of Lysosomal Enzymes: Application to Newborn Screening and Diagnosis of Mucopolysaccharidoses Types II, IVA, and VI." Clinical Chemistry 61, no. 11 (2015): 1363–71. http://dx.doi.org/10.1373/clinchem.2015.242560.

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Abstract BACKGROUND There is interest in newborn screening and diagnosis of lysosomal storage diseases because of the development of treatment options that improve clinical outcome. Assays of lysosomal enzymes with high analytical range (ratio of assay response from the enzymatic reaction divided by the assay response due to nonenzymatic processes) are desirable because they are predicted to lead to a lower rate of false positives in population screening and to more accurate diagnoses. METHODS We designed new tandem mass spectrometry (MS/MS) assays that give the largest analytical ranges repor

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Woon, James Sy-Keen, Mukram M. Mackeen, Rosli M. Illias, et al. "Cellobiohydrolase B ofAspergillus nigerover-expressed inPichia pastorisstimulates hydrolysis of oil palm empty fruit bunches." PeerJ 5 (October 12, 2017): e3909. http://dx.doi.org/10.7717/peerj.3909.

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BackgroundAspergillus niger, along with many other lignocellulolytic fungi, has been widely used as a commercial workhorse for cellulase production. A fungal cellulase system generally includes three major classes of enzymes i.e., β-glucosidases, endoglucanases and cellobiohydrolases. Cellobiohydrolases (CBH) are vital to the degradation of crystalline cellulose present in lignocellulosic biomass. However,A. nigernaturally secretes low levels of CBH. Hence, recombinant production ofA. nigerCBH is desirable to increase CBH production yield and also to allow biochemical characterisation of the r

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RESTAINO, LAWRENCE, ELON W. FRAMPTON, ROBERT M. IRBE, GÜNTER SCHABERT, and HANS SPITZ. "Isolation and Detection of Listeria monocytogenes Using Fluorogenic and Chromogenic Substrates for Phosphatidylinositol-Specific Phospholipase C." Journal of Food Protection 62, no. 3 (1999): 244–51. http://dx.doi.org/10.4315/0362-028x-62.3.244.

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The BCM Listeria monocytogenes detection system (LMDS) consists of a selective preenrichment broth (LMPEB), selective enrichment broth (LMSEB), selective/differential plating medium (LMPM), and identification on a confirmatory plating medium (LMCM). The efficacy of the BCM LMDS was determined using pure cultures and naturally and artificially contaminated environmental sponges. The BCM LMPEB allowed the growth of Listeria and resuscitation of heat-injured L. monocytogenes. The BCM LMSEB, which contains the fluorogenic substrate 4-methylumbelliferyl-myo-inositol-1-phosphate and detects phosphat

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