Purification, immobilization and kinetic characterization of G-x-S-x-G esterase with short chain fatty acid specificity from Lysinibacillus fusiformis AU01

Divakar, K.; M, Suryia Prabha; Pennathur, Gautam

doi:10.1016/j.bcab.2017.09.007

Cited by 11 publications

(1 citation statement)

References 53 publications

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“…The highest stability was achieved with acetonitrile, with which 281% of relative activities was retained in comparison to the untreated enzyme, followed by 2-propanol (195.6%). In other research, immobilized esterase from Lysinibacillus fusiformis AU01 maintained half of its relative activity in the presence of acetonitrile and 2-propanol [ 47 ]. The probable reason for the higher residual activity of the immobilized enzyme with acetonitrile compared to the corresponding free enzyme is the protection by the support material, thereby improving its structure sustainability against the solvent.…”

Section: Resultsmentioning

confidence: 99%

Immobilization of Hyperthermostable Carboxylesterase EstD9 from Anoxybacillus geothermalis D9 onto Polymer Material and Its Physicochemical Properties

et al. 2023

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Carboxylesterase has much to offer in the context of environmentally friendly and sustainable alternatives. However, due to the unstable properties of the enzyme in its free state, its application is severely limited. The present study aimed to immobilize hyperthermostable carboxylesterase from Anoxybacillus geothermalis D9 with improved stability and reusability. In this study, Seplite LX120 was chosen as the matrix for immobilizing EstD9 by adsorption. Fourier-transform infrared (FT-IR) spectroscopy verified the binding of EstD9 to the support. According to SEM imaging, the support surface was densely covered with the enzyme, indicating successful enzyme immobilization. BET analysis of the adsorption isotherm revealed reduction of the total surface area and pore volume of the Seplite LX120 after immobilization. The immobilized EstD9 showed broad thermal stability (10–100 °C) and pH tolerance (pH 6–9), with optimal temperature and pH of 80 °C and pH 7, respectively. Additionally, the immobilized EstD9 demonstrated improved stability towards a variety of 25% (v/v) organic solvents, with acetonitrile exhibiting the highest relative activity (281.04%). The bound enzyme exhibited better storage stability than the free enzyme, with more than 70% of residual activity being maintained over 11 weeks. Through immobilization, EstD9 can be reused for up to seven cycles. This study demonstrates the improvement of the operational stability and properties of the immobilized enzyme for better practical applications.

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Section: Resultsmentioning

confidence: 99%

Immobilization of Hyperthermostable Carboxylesterase EstD9 from Anoxybacillus geothermalis D9 onto Polymer Material and Its Physicochemical Properties

et al. 2023

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Thermoalkalophilic recombinant esterase entrapment in chitosan/calcium/alginate‐blended beads and its characterization

Tercan

Sürmeli

Şanlı‐Mohamed

2021

J of Chemical Tech & Biotech

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BACKGROUND: Esterases (EC 3.1.1.1), a class of hydrolases, degrade the ester bonds of lipids into alcohol and carboxylic acids and synthesize carboxylic ester bonds. They are used in a variety of biotechnological, industrial, environmental, and pharmaceutical applications due to their many valuable properties. Particularly, extremophilic esterases with many superior properties are of great interest for various reactions. Immobilization of enzymes may provide some advantages over free enzymes not only to improve the properties of enzymes but also to increase the reusability of biocatalyst in industrial applications. Therefore, many different immobilization applications for enzymes have been reported in various studies. To our knowledge, a thermophilic esterase has not so far been immobilized by entrapment using chitosan/calcium/alginate-blended beads. Here, we reported the immobilization of thermoalkalophilic recombinant esterase by entrapment using chitosan/calcium/alginateblended beads, and then the entrapped esterase was characterized biochemically in details.RESULTS: In the present study, a thermophilic recombinant esterase was immobilized by entrapment in chitosan/calcium/alginateblended beads for the first time. The 0.5 mg mL −1 purified recombinant esterase was entrapped in 1% chitosan, 2% alginate, and 0.7 M CaCl 2 blended beads. The results showed that immobilization yield and entrapment efficiency of the entrapped esterase were 69.5% and 80.4%, respectively. SEM micrograph showed that the surface of the beads resembled a mesh and very compact structures. Chitosan/calcium/alginate-blended beads exhibited an 18.8% swelling ratio and had a moderate porous structure. The entrapment technique highly enhanced the thermostability of the esterase and shifted its optimum temperature from 65 to 80°C. The immobilized esterase was very stable in a wide range of pH (8.5-11) displaying maximum activity at pH 9. ZnCl 2 slightly increased the activity of immobilized esterase whereas several metal ions reduced the enzyme activity. When the enzyme was immobilized in chitosan/calcium/alginate-blended beads, its K m increased about 2 times and V max value decreased almost 1.5 times. Immobilization allowed repeated uses of the esterase having good operational stability in a continuous process. CONCLUSION:The results revealed that the immobilization of a thermophilic recombinant esterase by entrapment in chitosan/ calcium/alginate-blended beads exhibited considerably better compared to other immobilization processes with various entrapment strategies.

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Purification, identification and characterization of an esterase with high enantioselectivity to (S)-ethyl indoline-2-carboxylate

et al. 2019

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Purification, immobilization and kinetic characterization of G-x-S-x-G esterase with short chain fatty acid specificity from Lysinibacillus fusiformis AU01

Cited by 11 publications

References 53 publications

Immobilization of Hyperthermostable Carboxylesterase EstD9 from Anoxybacillus geothermalis D9 onto Polymer Material and Its Physicochemical Properties

Immobilization of Hyperthermostable Carboxylesterase EstD9 from Anoxybacillus geothermalis D9 onto Polymer Material and Its Physicochemical Properties

Thermoalkalophilic recombinant esterase entrapment in chitosan/calcium/alginate‐blended beads and its characterization

Purification, identification and characterization of an esterase with high enantioselectivity to (S)-ethyl indoline-2-carboxylate

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