Production and characterization of thermo-, halo- and solvent-stable esterase from <i>Bacillus mojavensis</i> TH309

Adıgüzel, Ali Osman

doi:10.1080/10242422.2020.1715370

Cited by 22 publications

(6 citation statements)

References 64 publications

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“…4F. 64,75,76 These results are also in accordance to the in silico protein-ligand interaction. Molecular docking simulations performed for p-NP-butyrate indicated that specic bonding of esterase enzyme in this study with p-NP-butyrate occurred at arginine68 and serine226 of esterase as shown in Fig.…”

Section: Discussionsupporting

confidence: 86%

Heterologous expression, molecular studies and biochemical characterization of a novel alkaline esterase gene fromBacillus thuringiensisfor detergent industry

et al. 2022

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Section: Discussionsupporting

confidence: 86%

Heterologous expression, molecular studies and biochemical characterization of a novel alkaline esterase gene fromBacillus thuringiensisfor detergent industry

et al. 2022

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“…Nevertheless, psychrophilic and thermophilic halotolerant lipolytic enzymes were also detected. For example, 7N9 [ 42 ], lp_3505 [ 72 ], EstS [ 11 ], Est10 [ 88 ], and EstLiu [ 24 ] displayed a temperature optimum ranging from 0 to 30 °C, whereas E69 [ 76 ], Est9x [ 27 ], BmEST [ 89 ], and LipJ2 [ 39 ] exhibit their optimal activity between 60 and 80 °C. With respect to pH, most of the halotolerant enzymes including Est56 are moderate alkaliphilic, with the optimum pH between 7.5 and 9 ( Table S1 ).…”

Section: Discussionmentioning

confidence: 99%

A Novel Carboxylesterase Derived from a Compost Metagenome Exhibiting High Stability and Activity towards High Salinity

Daniel

2021

Genes

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Halotolerant lipolytic enzymes have gained growing interest, due to potential applications under harsh conditions, such as hypersalinity and presence of organic solvents. In this study, a lipolytic gene, est56, encoding 287 amino acids was identified by functional screening of a compost metagenome. Subsequently, the gene was heterologously expressed, and the recombinant protein (Est56) was purified and characterized. Est56 is a mesophilic (Topt 50 °C) and moderate alkaliphilic (pHopt 8) enzyme, showing high thermostability at 30 and 40 °C. Strikingly, Est56 is halotolerant as it exhibited high activity and stability in the presence of up to 4 M NaCl or KCl. Est56 also displayed enhanced stability against high temperatures (50 and 60 °C) and urea (2, 4, and 6 M) in the presence of NaCl. In addition, the recently reported halotolerant lipolytic enzymes were summarized. Phylogenetic analysis grouped these enzymes into 13 lipolytic protein families. The majority (45%) including Est56 belonged to family IV. To explore the haloadaptation of halotolerant enzymes, the amino acid composition between halotolerant and halophilic enzymes was statistically compared. The most distinctive feature of halophilic from non-halophilic enzymes are the higher content of acidic residues (Asp and Glu), and a lower content of lysine, aliphatic hydrophobic (Leu, Met and Ile) and polar (Asn) residues. The amino acid composition and 3-D structure analysis suggested that the high content of acidic residues (Asp and Glu, 12.2%) and low content of lysine residues (0.7%), as well as the excess of surface-exposed acidic residues might be responsible for the haloadaptation of Est56.

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“…For instance, Candida antarctica lipase B (Cal B) acts as a lipase when adsorbed to an acylglyceride interface and as TA B L E 3 Some esterase producing extremophiles an esterase when exposed to an aqueous environment (Benson & Pleiss, 2017). Several microbial esterases from extreme environments (Table 3) are very active at low and high temperature, salt concentration, and pH (Adıgüzel, 2020;Curci et al, 2019;Jiang, Zhang, Gao, & Hu, 2016;Polkade, Ramana, Joshi, Pardesi, & Shouche, 2015;Wang, Wang, Cao, & Zhu, 2016;Zarafeta et al, 2016).…”

Section: Esterasesmentioning

confidence: 99%

Revisiting the scope and applications of food enzymes from extremophiles

Akanbi

Agyei

2020

J. Food Biochem.

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Production and characterization of thermo-, halo- and solvent-stable esterase from Bacillus mojavensis TH309

Cited by 22 publications

References 64 publications

Heterologous expression, molecular studies and biochemical characterization of a novel alkaline esterase gene fromBacillus thuringiensisfor detergent industry

Heterologous expression, molecular studies and biochemical characterization of a novel alkaline esterase gene fromBacillus thuringiensisfor detergent industry

A Novel Carboxylesterase Derived from a Compost Metagenome Exhibiting High Stability and Activity towards High Salinity

Revisiting the scope and applications of food enzymes from extremophiles

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