Purification and characterization of a novel thermostable esterase from Thermus sp. NCCB 100425T

Akatin, Melike Yildirim

doi:10.5505/tjb.2015.13008

Cited by 3 publications

(4 citation statements)

References 37 publications

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“…Esterase produced by a ruminal bacterium But-yrivibrio fibrisolvens degraded substrates at a rate in the order 1-naphthyl acetate > 1-naphthyl butyrate > 1-naphthyl propionate but did not degrade 1-naphthyl palmitate or 1-naphthyl phosphate 17. The purified esterase from Thermus sp. NCCB 100425 T had maximal relative activity towards p-NPA and p-NPB, respectively, whereas it could slightly cleavage ester bonds of p-NPL and p-NPP 26.…”

Section: Substrate Specificity Of Esterase Of B Safensis Strainmentioning

confidence: 96%

Optimization and Partial Purification of an Extracellular Esterase Produced by a Bacillus safensis Strain Isolated from Ear Wax

Gupta,

S Kanwar

2016

J. Adv. Mircobiol.

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The esterases catalyzing the hydrolysis of acyl esters are highly desired in industrial applications. An extracellular esterase producing, mesophilic and alkaliphilic Gram positive bacterial isolate obtained from human ear wax (sebum) was identified as Bacillus safensis strain. The B. safensis strain produced relatively higher amount of esterase after 36 h at 37 o C under shaking conditions when coconut oil (1.75 %, v/ v) and gelatin (0.6 %, w/v) were used in the Mineral-Based broth as carbon and nitrogen source, respectively. The esterase production by B. safensis strain increased by ~208 % by consecutive optimization of physicochemical parameters. The esterase was partially purified by acetone precipitation. Enzyme showed greater affinity towards a relatively short C-chain ester p-NPA as substrate. The K m and V max values of the esterase were found to be 0.127 mM and 8.82 U/ml/min, respectively. The esterase was purified up to 2.8 fold by acetone precipitation (20-40 % saturation). The esterase was found to be a heptameric protein of 49 kDa (under native-PAGE) comprising seven units of 4 7 kDa as revealed by SDS-PAGE.

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Section: Substrate Specificity Of Esterase Of B Safensis Strainmentioning

confidence: 96%

Optimization and Partial Purification of an Extracellular Esterase Produced by a Bacillus safensis Strain Isolated from Ear Wax

Gupta,

S Kanwar

2016

J. Adv. Mircobiol.

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“…Est1 was found to be 0.095 mM [14], Km of Thermoanaerobacterium thermosaccharolyticum esterase was 3.337 mM [16], Km of Thermus sp. NCCB 100425T esterase was 18.32 mM [17], Km of Geobacillus sp. DF20 esterase was 0.12 mM [13], Km of Geobacillus sp.…”

Section: Kinetic Parametersmentioning

confidence: 96%

“…Est1 and Est3 is 9.5 [14] and the optimum pH of Thermus sp. NCCB 100425T is 7.5 [17]. Carboxylesterases in the literature generally have high optimum pHs.…”

Section: (A) (B)mentioning

confidence: 99%

Characterization of a New Thermostable Carboxylesterase from Aneurinibacillus sp. PDF24

KOLCU

Şal

Beldüz

et al. 2022

Sakarya University Journal of Science

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In this study, esterase of Aneurinibacillus sp. PDF24 strain, a thermophilic bacteria, was purified to homogenity (5.25 fold purification) by column chromotography, and characterized. The molecular weight of Aneurinibacillus sp. PDF24 esterase was determined about 40 kDa. The maximum activity of the purified esterase was analyzed at 55 °C, pH 8.5. The esterase was found to be stable at 40 ºC, 50 ºC and 60 ºC for 1 hour. Km and Vmax values for p-nitrophenyl butyrate were determined as 0.120 mM and 3164.8 U/mg, respectively. In the presence of 1 mM and 5 mM metal salts of Mg2+, Li+, Ca2+, K+, no significant change occured in enzyme activity, The activity of Aneurinibacillus sp PDF24 esterase was found to be stable also in the presence of ethanol, DMSO, EDTA, DTT and ß-mercaptoethanol. The data obtained suggest that the enzyme is a serine esterase, not a metalloprotein, and that disulfide bonds are not required to maintain enzyme conformation, and therefore, depending on its features, this esterase may be a suitable candidate for industrial applications.

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“…The biodegradation assay media of isolates InaCC B538 and B947 were measured for esterase activity using the method of Tekincanli et al (2015) and Shin et al (2021). The biodegradation assay medium was centrifuged at 6,000 rpm for 5 min to obtain the enzyme sample in the supernatant.…”

Section: Esterase Activity Assaymentioning

confidence: 99%

The Potential of Bacillus altitudinis B538 and Alcaligenes faecalis B947 in PET and PCL Plastic Degradation

Dini,

Nurcholis,

Ulfah

et al. 2024

HAYATI J Biosci

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Polyethylene terephthalate (PET) plastic is the most widely used type of plastic that produces waste and causes various environmental and health problems. The treatment of PET plastic waste with chemically and mechanically recycling approaches still has shortcomings, so biological processing using microorganisms or enzymes has new potential. Two bacterial isolates from the Indonesian Culture Collection of National Research and Innovation Agency (InaCC, BRIN), namely isolate InaCC B538 and InaCC B947, were further observed for their potential in PET plastic degradation. Firstly, both isolates were determined by the molecular marker 16S rDNA. The potential of both isolates was measured with following method: 10 days of degradation using PET and PCL substrates, esterase enzyme activity assay, and observation of the PET plastic surface using Scanning Electron Microscope (SEM). Species identification was performed using DNA sequencing of 16S rDNA. InaCC B538 and InaCC B947 were closely related to Bacillus altitudinis TBMAX41 and Alcaligenes faecalis AN-13, respectively. InaCC B947 isolate has a better potential in degrading PET plastic and PCL with a degradation percentage of 0.32% for PET plastic and 3.22% for PCL film for 10 days, respectively, and esterase activity of 0.06 U/ml; while InaCC B538 did not cause weight loss of PET and 2.49% for PCL, respectively, with esterase activity of 0.04 U/ml. The degradation of PET plastic by the isolates InaCC B947 was able to cause damage to the plastic surface leading to the degradation of PET plastic.

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Purification and characterization of a novel thermostable esterase from Thermus sp. NCCB 100425T

Cited by 3 publications

References 37 publications

Optimization and Partial Purification of an Extracellular Esterase Produced by a Bacillus safensis Strain Isolated from Ear Wax

Optimization and Partial Purification of an Extracellular Esterase Produced by a Bacillus safensis Strain Isolated from Ear Wax

Characterization of a New Thermostable Carboxylesterase from Aneurinibacillus sp. PDF24

The Potential of Bacillus altitudinis B538 and Alcaligenes faecalis B947 in PET and PCL Plastic Degradation

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