Immobilized enzymes: a comprehensive review

Khan, Mohammad Rafiq

doi:10.1186/s42269-021-00649-0

Cited by 53 publications

(27 citation statements)

References 55 publications

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“…3B, the maximum relative activity of free enzyme was achieved at the temperature of 50°C, and it became less stable at higher temperatures. CALA exhibited a higher residual catalytic activity after covalent binding to the support, which could be attributed to the reduction of its conformational exibility and the diffusional limitation of the carrier [Khan et al 2021]. A signi cant enhancement in the thermal stability of the enzyme was also observed in the in situ immobilization, especially at temperatures of 70°C, with about 40% improvement of the relative activity.…”

Section: Temperature and Ph Stability Of The Free And Immobilized Der...mentioning

confidence: 96%

Comparison of covalent and in-situ immobilization of Candida antarctica lipase A on a flexible nanoporous material

Ghasemi

Yousefi²,

Nikseresht

2022

Preprint

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In this study, Candida antartica lipase A (CALA) was subjected to immobilization on the flexible nanoporous MIL-53(Fe) by two approaches: covalent coupling and in situ immobilization method. The pre-synthesized support under ultrasound irradiation was incubated with N,N-dicyclohexylcarbodiimide to mediate the covalent attachment between the carboxylic groups on the support surface and amino groups of enzyme molecules. The in situ immobilization in which the enzyme molecules directly embedded into the MOF framework was performed under mild operating conditions in a facile one-step manner. Both immobilized derivatives of the enzyme were characterized by scanning electron microscopy (SEM), X-ray diffraction (XRD), thermogravimetric analysis (TGA), FT-IR spectra, and energy-dispersive X-ray spectroscopy (EDS). In the in situ immobilization method, the enzyme molecules were efficiently encapsulated within the support with high loading capacity (220 mg/g support). On the other hand, the covalent attachment resulted in immobilizing much lower concentrations of the enzyme (20 mg/g support). Although both immobilized derivatives of lipase showed broader pH and temperature tolerance relative to the soluble enzyme, the biocatalyst, which was prepared through in situ method, was more stable at elevated temperatures than the covalently immobilized lipase. Furthermore, in-situ immobilized derivatives of CALA could be efficiently reused for at least eight cycles (> 70% of retained activity). In contrast, its covalently immobilized counterpart showed a drastic decrease in activity after five cycles (less than 10% of retained activity at the end of 6 rounds).

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Section: Temperature and Ph Stability Of The Free And Immobilized Der...mentioning

confidence: 96%

Comparison of covalent and in-situ immobilization of Candida antarctica lipase A on a flexible nanoporous material

Ghasemi

Yousefi²,

Nikseresht

2022

Preprint

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“…Additionally, with enhanced stability, immobilized enzymes can be reused for repeated cycles. 71,72 Therefore, these advantages prompt their applications in, among others, esterification and transesterification reactions.…”

Section: Esters With Lubricating and Fuel Propertiesmentioning

confidence: 99%

Fusel Oil: Chemical Composition and an Overview of Its Potential Application

Massa¹,

Raspe²,

Feiten³

et al. 2023

J. Braz. Chem. Soc.

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Fusel oil (FO) is one of the by-products of the sugar-alcohol industry, which has application as an additional source of higher alcohols for production of esters with flavoring, fuels and lubricants properties, as well as additives in petroleum-based fuels and in pesticide formulations. Thus, this review is focused on the characteristics of FO and its applications as an acyl acceptor in transesterification and esterification reactions for esters production, its addition to fossil fuels, and the herbicidal and fungicidal potential of the compounds presented in its chemical composition. The operating conditions of the process, results obtained, and patented applications in the food, cosmetic, transportation and agricultural sectors are also reported and discussed. Furthermore, main trends, challenges and recommendations are proposed in order to overcome the disadvantages of applying FO in the reported sectors, as well as alternatives for the development of new lines of research are suggested.

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“…Besides catalytic activity, in large scale bioprocesses, the catalyst operational stability is very important, and along with the modulation of enzyme selectivity and activity, the necessity to improve the stability of enzymes and to metamorphose them into stable, robust, recyclable catalysts has become critical. [26][27][28][29][30][31][32][33][34] Lipase B from Candida antarctica (CaL-B) possesses a high lipolytic activity 35,36 and is used in important biomedical applications. [37][38][39][40][41][42][43][44][45] Due to its properties such as high selectivity, large substrate domain, and high tolerance to temperature and organic solvents, [46][47][48] CaL-B is well known as a catalyst in the kinetic resolution processes of secondary chiral ethanols, 49 including phenothiazine bearing alcohols allowing the preparation of enantiomerically enriched stereoisomers.…”

Section: Introductionmentioning

confidence: 99%