Characterization of esterases from Cucurbita pepo cv. "Eskandrani"

Bioresource Technology

Volumn 99, Issue 2, 2008, Pages 437-443

  Fahmy, Afaf S ^a   Abo Zeid, Amal Z ^a   Mohamed, Tarek M ^b   Ghanem, Hala M ^c   Borai, Ibrahim H ^c   Mohamed, Saleh A ^a  

^a NATIONAL RESEARCH CENTRE   (Egypt)

^b TANTA UNIVERSITY   (Egypt)

^c Ain Shams University   (Egypt)

Author keywords

Characterization; Cucurbita pepo cv. "Eskandrani"; Esterase; Purification

Indexed keywords

CARBON ATOM; CUCURBITA PEPO CV; ESTERASE;

CARBON; CHARACTERIZATION; CHROMATOGRAPHY; ENZYMES; FILTRATION; GELS; MOLECULAR WEIGHT; MONOMERS; PH EFFECTS; PURIFICATION;

ESTERS;

4 NITROPHENYLPHOSPHATASE; BACTERIAL ENZYME; CARBON; CYSTEINE; ESKANDRANI; ESTERASE; METAL ION; SERINE; UNCLASSIFIED DRUG;

CARBON; CHARACTERIZATION; CHROMATOGRAPHY; ENZYMES; ESTERS; FILTRATION; GELS; MOLECULAR WEIGHT; MONOMERS; PH EFFECTS; PURIFICATION;

CATION; ENZYME ACTIVITY; HERB; HOMOGENEITY; INHIBITOR; METAL;

ANION EXCHANGE CHROMATOGRAPHY; ARTICLE; BINDING AFFINITY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; FOOD INDUSTRY; FOOD PROCESSING; GEL FILTRATION CHROMATOGRAPHY; INCUBATION TEMPERATURE; MOLECULAR WEIGHT; PH; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; SQUASH; THERMOSTABILITY;

CHROMATOGRAPHY; CHROMATOGRAPHY, GEL; CUCURBITA; ESTERASES; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR WEIGHT; PROTEIN SUBUNITS;

CUCURBITA PEPO;

EID: 35448948203     PISSN: 09608524     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biortech.2006.11.062     Document Type: Article

References (40)

1. Baigori M.D., Castor G.R., and Sineriz F. Purification and characterization of an extracellular esterase from Bacillus subtilis MIR-16. Biochemistry 24 (1996) 7-11
2. Bhowmik T., and Marth E.H. Esterases of Micrococcus species: identification and partial characterization. J. Dairy Sci. 73 (1990) 33-40
3. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
4. Carino L.A., and Montgomery M.W. Identification of some soluble esterases of the carrot (Daucus carota L.). Phytochemistry 7 (1968) 1483-1490
5. Chao Y.-P., Fu H., Wang Y.-L., Huang W.-B., and Wang J.-Y. Molecular cloning of the carboxylesterase gene and biochemical characterization of the encoded protein from Pseudomonas citronellolis ATCC 13674. Res. Microbiol. 154 (2003) 521-526
6. Davis B.J. Disc electrophoresis. Method and application to human serum proteins. Ann. N.Y. Acad. Sci. 121 (1964) 404-427
7. Desborough S., and Peloquin S.J. Disc electrophoresis of tuber proteins from Solanum species and interspecific hybrids. Phytochemistry 5 (1966) 727-733
8. Fenster K.M., Parkin K.L., and Steele J.L. Characterization of an arylesterase from Lactobacillus helveticus CNRZ32. J. Appl. Microbiol. 88 (2000) 572-583
9. Fuchs C., Vine N., and Hills M.J. Purification and characterization of the acid lipase from the endosperm of castor oil seeds. J. Plant Physiol. 149 (1996) 23-29
10. Fujikura Y., and Baisted D. Purification and characterization of basic lysophospholipase in germinating barley. Arch. Biochem. Biophys. 243 (1985) 570-578
11. Galliard T., and Dennis S. Isoenzymes of lipolytic acyl hydrolase and esterase in potato tuber. Phytochemistry 13 (1974) 2463-2468
12. Gobbetti M., Smacchi E., and Corsetti A. Purification and characterization of a cell surface-associated esterase from Lactobacillus fermentum DT41. Int. Dairy J. 7 (1997) 13-21
13. Goodenough P.W., and Entwistle T.G. The hydrodynamic properties and kinetic constants with natural substrates of the esterase from Malus pumila fruit. Eur. J. Biochem. 127 (1982) 145-149
14. Gu Q.M., Chen C.S., and Sih C.J. A facile enzymatic resolution process for the preparation of (+) S 2 (6 methoxy 2 naphthyl) propionic acid (Naproxen). Teterahed. Lett. 27 (1986) 1763-1766
15. Gupta A.K., and Kazlauskas R.J. Substrate modification to increase the enantioselectively of hydrolases a route to optically active cyclic allylic alcohols. Tetrahedron-Asymmetry 4 (1993) 879-888
16. Hatzinikolaou D.G., Kourentzi E., Stamatis H., Christakopoulos P., Kolisis F.N., Kekos D., and Nacris B.J. A novel lipolytic activity of Rhodotorula glutinis cells: production, partial characterization and application in the synthesis of esters. J. Biosci. Bioeng. 88 (1999) 53-56
17. Hinrichsen L.L., Montel M.C., and Talon R. Proteolytic and lipolytic activities of Mirococcus roseus (65), Halomonas elongata (16) and Vibrio sp. (168) isolated from Danish bacon curing brines. Int. J. Food Microbiol. 22 (1994) 115-126
18. Hou W.-C., Chen H.-J., Chang C.-F., and Lin Y.-H. Purification and properties of fatty acid esterases from yam (Dioscorea batatas Decne) tuber. Bot. Bull. Acad. Sinica 40 (1999) 305-310
19. James D.J., and Smith A.R.W. A biochemical study of non-specific esterases from plant cells, employing the histochemical substrate naphthol AS-D acetate. Histochem. J. 6 (1974) 7-23
20. Janssen P.H., Monk C.R., and Morgan H.W. A thermophilic, lipolytic Bacillus sp. and continuous assay of its p-nitrophenyl-palmitate esterase activity. FEMS Microbiol. Lett. 120 (1994) 195-200
21. Kademi A., Ait-Abdelkader N., Fakhreddine L., and Baratti J.C. Characterization of a new thermostable esterase from the moderate thermophilic bacterium Bacillus circulans. J. Mol. Catal. B: Enzyme 10 (2000) 395-401
22. Laemmli U.K. Cleavage of structural proteins during the assembly of the head bacteriophage T4. Nature 227 (1970) 680-685
23. Lee S.Y., and Lee B.H. Esterolytic and lipolytic activities of Lactobacillus casei-subsp.-casei- LLG. J. Food Sci. 55 (1990) 119-122
24. Liu S.-Q., Holland R., and Crow V.L. Purification and properties of intracellular esterases from Streptococcus thermophilus. Int. Dairy J. 11 (2001) 27-35
25. McKay A.M. Microbial carboxylic ester hydrolases (EC 3.1.1) in food biotechnology. Lett. Appl. Microbiol. 16 (1993) 1-6
26. Mohamed M.A., Mohamed T.M., Mohamed S.A., and Fahmy A.S. Distribution of lipases in the Gramineae. Partial purification and characterization of esterase from Avena fatua. Biores. Technol. 73 (2000) 227-234
27. Mukherjee K.D. Plant lipases and their application in lipid biotransformations. Prog. Lipid Res. 33 (1994) 165-174
28. Nourse A., Schabort J.C., Dirr H.W., and Dubery I.A. Purification and properties of an esterase from Cucurbita maxima fruit tissue. Phytochemistry 28 (1989) 379-383
29. Okeno J.A., and Ayiecho P.O. Isozyme variation among Amaranthus cultivars. Discov. Innovat. 8 (1996) 151-158
30. Oterholm A., Witter L.D., and Ordal J.Z. Purification and properties of an acetyl ester hydrolase (acetylesterase) from Lactobacillus plantarum. J. Dairy Sci. 55 (1972) 8
31. Ozaki E., Uragaki T., Sakashita K., and Sakimae A. Enzymatic preparation of alkanedicarboxylic acid monoesters. Chem. Lett. 7 (1995) 539-540
32. Rajeshwara A.N., and Prakash V. Purification and characterization of lipase from rice (Oryza sativa L.) bran. Nahrung 39 (1995) 406-418
33. Rudolph K., and Stahmann M.A. Multiple hydrolases in bean leaves (Phaseolus vulgaris L.) and the effect of the halo blight disease caused by Pseudomonas phaseolicola (Burkh.) Dowson. Plant Physiol. 41 (1966) 389-394
34. Schwartz H.M., Biedron S.I., Von Holdt M.M., and Rehm S. A study of some plant esterases. Phytochemistry 3 (1964) 189-200
35. Staubmann R., Ncube I., Gubitz G.M., Steiner W., and Read J.S. Esterase and lipase activity in Jatropha curcas L. seeds. J. Biotechnol. 75 (1999) 117-126
36. Stuhlfelder C., Lottspeich F., and Mueller M.J. Purification and partial amino acid sequences of an esterase from tomato. Phytochemistry 60 (2002) 233-240
37. Suh H.S., Sato Y.I., and Morishima H. Genetic characterization of weedy rice (Oryza sativa L.) based on morpho-physiology, isozymes and RAPD markers. Theor. Appl. Genet. 94 (1997) 316-321
38. Veerabhadrappa P.S., and Montgomery M.W. Polyacrylamide-gel electrophoresis of pea and garden bean carboxylesterases. Phytochemistry 10 (1971) 1171-1174
39. Wood A.N.P., Fernandez-Lafuente R., and Cowan D.A. Purification and partial characterization of a novel thermophilic carboxylesterase with high mesophilic specific activity. Enzyme Microb. Technol. 17 (1995) 816-825
40. Zock J., Cantwell C., Swartling J., Hodges R., Pohl T., Sutton K., Rosteck Jr. P., McGilvray D., and Queener S. The Bacillus subtillus pnbA gene encoding p-nitrobenzyl esterase: cloning sequence and high-level expression in Escherichia coli. Gene 151 (1994) 37-43