High throughput synthesis of ethyl pyruvate by employing superparamagnetic iron nanoparticles-bound esterase

Sharma, Abhishek; Sharma, Taruna; Meena, Khem Raj; Kumar, Ashok; Kanwar, Shamsher S.

doi:10.1016/j.procbio.2018.05.004

Cited by 25 publications

(16 citation statements)

References 39 publications

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“…46 Additionally, free esterase from Bacillus pumilus and its immobilized form on silane functionalized superparamagnetic nanoparticles (SNPs) had maximum activity at 37 and 45°C, respectively. 47 The esterase from Lysinibacillus fusiformis AU01 showed maximum activity at 40°C for free enzyme and at 45°C for immobilized enzyme onto celite545 with 3-aminopropyltriethoxysilane as a linker molecule. 48 Besides, free and immobilized Mucor miehei esterase on core-shell magnetic beads via adsorption and covalent binding showed an optimal temperature at 40 and 50°C, respectively.…”

Section: The Influence Of Temperature and Phmentioning

confidence: 99%

“…9 There have been some recent reports with similar results on immobilized esterases using different techniques, showing at least 70% of residual activity after three sequential cycles. 45,47,53,55,59,60 The influence of bead size The effect of bead sizes (1.8, 2.6, and 3.9 mm) was investigated on the activity of the immobilized enzyme. This analysis results showed that the highest esterase activity was determined at 1.8 mm diameter beads the smallest size obtained in the present study (Fig.…”

Section: Kinetic Studiesmentioning

confidence: 99%

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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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Section: The Influence Of Temperature and Phmentioning

confidence: 99%

Section: Kinetic Studiesmentioning

confidence: 99%

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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“…Furthermore, a decrease in the CA activity was noticed with a further increase in temperature (Fig. 5 (b)) [24]. The decrease in activity might be attributed to the denaturation of protein at a higher temperature.…”

Section: Optimization Of Production Conditions For Camentioning

confidence: 81%

“…The reaction mixture was again incubated at 37°C in a water bath for 5 min [23]. The amount of p-nitrophenol released was measured at 410 nm after 5-min incubation using a microplate reader (Thermo-scientific, Multiskan™ FC Microplate Photometer) [24]. Based on CA activity, a potent isolate T5 was selected for all subsequent studies.…”

Section: Enzyme Assaymentioning

confidence: 99%

Efficient reduction of CO2 using a novel carbonic anhydrase producing Corynebacterium flavescens

Sharma

Kumar

2020

Environmental Engineering Research

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Emission of greenhouse gases into the atmosphere by human activities leads to global warming. To reduce the level of CO2 the bio-catalytic properties of microbial carbonic anhydrase (CA) can be exploited. The present study aimed to isolate CA producing bacteria from cow saliva. After thorough screening for CA activity in the bacterial cultures, ten isolates were selected. Out of ten bacterial isolates, T5 isolate showed the highest CA activity (83.92 U/mL) and the isolate was identified as Corynebacterium flavescens using 16s rRNA analysis. Various production parameters for the optimum production of CA were optimized. During the optimization, incubation temperature 40°C, agitation speed 120 rpm, and inoculum volume 4%v/v was found to be optimum for CA production. The optimum reaction pH, reaction time and temperature were 7, 10 min and 35°C, respectively. The crude enzyme was tested for the conversion of CO2 into the calcium carbonate (CaCO3) under controlled conditions. The CO2 conversion efficacy of crude CA was observed to be ~45 mg CaCO3/mg protein. The synthesized CaCO3 was analyzed using scanning electron microscopy and X-ray diffraction techniques for particle size, morphology and elemental structure. Calcite precipitation by bacterial CA makes it a potential candidate to be effectively employed in biomimetic CO2 sequestration.

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“…Also, the functional moiety on the biocatalyst surface gives an idea about which type of interaction takes place between the enzyme and matrix. Furthermore, the efficiency of polymeric matrices can be enhanced by surface functionalization [ 25 ]. The surface modification allows the addition of a particular functional group onto the surface of the polymeric matrix to attain the desired properties.…”

Section: Introductionmentioning

confidence: 99%

Mechano-chemical and biological energetics of immobilized enzymes onto functionalized polymers and their applications

et al. 2022

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Enzymes of commercial importance, such as lipase, amylase, laccase, phytase, carbonic anhydrase, pectinase, maltase, glucose oxidase etc ., show multifunctional features and have been extensively used in several fields including fine chemicals, environmental, pharmaceutical, cosmetics, energy, food industry, agriculture and nutraceutical etc . The deployment of biocatalyst in harsh industrial conditions has some limitations, such as poor stability. These drawbacks can be overcome by immobilizing the enzyme in order to boost the operational stability, catalytic activity along with facilitating the reuse of biocatalyst. Nowadays, functionalized polymers and composites have gained increasing attention as an innovative material for immobilizing the industrially important enzyme. The different types of polymeric materials and composites are pectin, agarose, cellulose, nanofibers, gelatin, and chitosan. The functionalization of these materials enhances the loading capacity of the enzyme by providing more functional groups to the polymeric material and hence enhancing the enzyme immobilization efficiency. However, appropriate coordination among the functionalized polymeric materials and enzymes of interest plays an important role in producing emerging biocatalysts with improved properties. The optimal coordination at a biological, physical, and chemical level is requisite to develop an industrial biocatalyst. Bio-catalysis has become vital aspect in pharmaceutical and chemical industries for synthesis of value-added chemicals. The present review describes the current advances in enzyme immobilization on functionalized polymers and composites. Furthermore, the applications of immobilized enzymes in various sectors including bioremediation, biosensor and biodiesel are also discussed.

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High throughput synthesis of ethyl pyruvate by employing superparamagnetic iron nanoparticles-bound esterase

Cited by 25 publications

References 39 publications

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

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

Efficient reduction of CO2 using a novel carbonic anhydrase producing Corynebacterium flavescens

Mechano-chemical and biological energetics of immobilized enzymes onto functionalized polymers and their applications

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