Characterization of esterases from Cucurbita pepo cv. “Eskandrani”

Fahmy, Afaf S.; Abo-Zeid, Amal Z.; Mohamed, Tarek M.; Ghanem, Hala M.; Borai, Ibrahim H.; Mohamed, Saleh A.

doi:10.1016/j.biortech.2006.11.062

Cited by 30 publications

(35 citation statements)

References 37 publications

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“…The addition of 10 mM Zn 2+ and Cu 2+ to the reaction mixture almost completely inhibited the enzyme activity (Table 2). Similar results have been reported for the esterases Cucurbita pepo [30] whereas the esterases from deep sea metagenomic library [19] and Acinetobacter baumannii BD5 [40] lost their activity more than 55% in the presence of Zn 2+ and Cu 2+ at 10 mM concentration.…”

Section: +supporting

confidence: 85%

“…This is similar to earlier findings shown for Penicillium chrysogenum [26], Aspergillus niger [27,28] and Aspergillus oryzae [29] esterases. However, the optimum temperature of Geobacillus sp TF17 esterase is higher than the esterases from Cucurbita pepo Elc and Ell with an optimum temperature between 30 and 40°C [30] and some Bacillus sp. with an optimum temperature at 45°C [17], and is lower than the esterase from Bacillus licheniformis S-86 [31] at 60°C and Fervidobacterium nodosum Rt17-B1 [32] at 75°C.…”

Section: Effect Of Ph and Temperature On Enzyme Activitymentioning

confidence: 88%

“…However, Mn 2+ , Co 2+ and Ca 2+ at 10 mM concentration reduced original esterase activity more than 40%. T. terreum [37], C. pepo [30] and B. subtilis RRL 1789 [38] esterases were inhibited by Mn…”

Section: Effect Of Some Metal Ions On the Enzyme Activitymentioning

confidence: 98%

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Purification and characterization of a pH and heat stable esterase from Geobacillus sp. TF17

Çolak

2013

Turk J Bioch

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Section: +supporting

confidence: 85%

Section: Effect Of Ph and Temperature On Enzyme Activitymentioning

confidence: 88%

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Purification and characterization of a pH and heat stable esterase from Geobacillus sp. TF17

Çolak

2013

Turk J Bioch

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“…The energy of activation of ME-III is 15.9495 kJ/mole and that of ME-IV is 14.59 kJ/mole, respectively. The optimum temperature obtained for other plant carboxylesterases such as barley, finger millet, S. grantii and Cucurbita pepo was also in the above range (Burger et al, 1970;Upadhya et al, 1985;Govindappa et al, 1987;Fahmy et al, 2008).…”

Section: Optimum Temperature and Temperature Stabilitymentioning

confidence: 86%

“…They have been purified from various plant sources including finger millet (Eleusine coracana) (Upadhya et al, 1985), Cucurbita maxima fruit tissue (Nourse et al, 1989), Jatropa curcas L. seeds (Staubmann et al, 1999), Avena fatua (Mohamed et al, 2000), tomato (Stuhlfelder et al, 2002) and Cucurbita pepo (Afaf S Fahmy et al, 2008) by employing different purification processes including ammonium sulphate fractionation, ion exchange chromatography and gel filtration chromatography. However, not all preparations have been shown to be homogeneous.…”

Section: Purificationmentioning

confidence: 99%

Carboxylesterases from the seeds of an underutilized legume, Mucuna pruriens; isolation, purification and characterization

2011

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a b s t r a c tTwo carboxylesterases (ME-III and ME-IV) have been purified to apparent homogeneity from the seeds of Mucuna pruriens employing ammonium sulfate fractionation, cation exchange chromatography on CMcellulose, gel-permeation chromatography on Sephadex G-100 and preparative PAGE. The homogeneity of the purified preparations was confirmed by polyacrylamide gel electrophoresis (PAGE), gel-electrofocussing and SDS-PAGE. The molecular weights determined by gel-permeation chromatography on Sephadex G-200 were 20.89 kDa (ME-III) and 31.62 kDa (ME-IV). The molecular weights determined by SDS-PAGE both in the presence and absence of 2-mercaptoethanol were 21 kDa (ME-III) and 30.2 kDa (ME-IV) respectively, suggesting a monomeric structure for both the enzymes. The enzymes were found to have Stokes radius of 2.4 nm (ME-III) and 2.7 nm (ME-IV). The isoelectric pH values of the enzymes, ME-III and ME-IV, were 6.8 and 7.4, respectively. ME-III and ME-IV were classified as carboxylesterases employing PAGE in conjunction with substrate and inhibitor specificity. The K m of ME-III and ME-IV with 1-naphthyl acetate as substrate was 0.1 and 0.166 mM while with 1-naphthyl propionate as substrate the K m was 0.052 and 0.0454 mM, respectively. As the carbon chain length of the acyl group increased, the affinity of the substrate to the enzyme increased indicating hydrophobic nature of the acyl group binding site. The enzymes exhibited an optimum temperature of 45°C (ME-III) and 37°C (ME-IV), an optimum pH of 7.0 (ME-III) and 7.5 (ME-IV) and both the enzymes (ME-III and ME-IV) were stable up to 120 min at 35°C. Both the enzymes were inhibited by organophosphates (dichlorvos and phosphamidon), but resistant towards carbamates (carbaryl and eserine sulfate) and sulphydryl inhibitors (p-chloromercuricbenzoate, PCMB).

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Esterases as emerging biocatalysts: Mechanistic insights, genomic and metagenomic, immobilization, and biotechnological applications

Rafeeq

Hussain

Shabbir

et al. 2021

Biotech and App Biochem

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Esterase enzymes are a family of hydrolases that catalyze the breakdown and formation of ester bonds. Esterases have gained a prominent position in today's world's industrial enzymes market. Due to their unique biocatalytic attributes, esterases contribute to environmentally sustainable design approaches, including biomass degradation, food and feed industry, dairy, clothing, agrochemical (herbicides, insecticides), bioremediation, biosensor development, anticancer, antitumor, gene therapy, and diagnostic purposes. Esterases can be isolated by a diverse range of mammalian tissues, animals, and microorganisms. The isolation of extremophilic esterases increases the interest of researchers in the extraction and utilization of these enzymes at the industrial level. Genomic, metagenomic, and immobilization techniques have opened innovative ways to extract esterases and utilize them for a longer time to take advantage of their beneficial activities. The current study discusses the types of esterases, metagenomic studies for exploring new esterases, and their biomedical applications in different industrial sectors.

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Characterization of esterases from Cucurbita pepo cv. “Eskandrani”

Cited by 30 publications

References 37 publications

Purification and characterization of a pH and heat stable esterase from Geobacillus sp. TF17

Purification and characterization of a pH and heat stable esterase from Geobacillus sp. TF17

Carboxylesterases from the seeds of an underutilized legume, Mucuna pruriens; isolation, purification and characterization

Esterases as emerging biocatalysts: Mechanistic insights, genomic and metagenomic, immobilization, and biotechnological applications

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