Chemical amination of Rhizopus oryzae lipase for multipoint covalent immobilization on epoxy-functionalized supports: Modulation of stability and selectivity

Ashjari, Maryam; Mohammadi, Mehdi; Badri, Rashid

doi:10.1016/j.molcatb.2015.02.011

Cited by 39 publications

(23 citation statements)

References 31 publications

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“…Among these groups, epoxy moieties are the most extensively applied for covalent binding of lipases because epoxy moieties carry simple groups for covalent binding and contain abundant active amino, phenolic, and thiol groups at a specific pH condition. Epoxy moieties have short spacer arms that are highly stable at pH 7.0 and that can support the enzyme on the surface of particles, thereby reducing steric hindrance of some immobilization enzymes and improving the whole catalytic activity [17,[19][20][21][22].…”

Section: Introductionmentioning

confidence: 99%

Immobilization of a Novel ESTBAS Esterase from Bacillus altitudinis onto an Epoxy Resin: Characterization and Regioselective Synthesis of Chloramphenicol Palmitate

et al. 2019

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Novel gene estBAS from Bacillus altitudinis, encoding a 216-amino acid esterase (EstBAS) with a signal peptide (SP), was expressed in Escherichia coli. EstBASΔSP showed the highest activity toward p-nitrophenyl hexanoate at 50 °C and pH 8.0 and had a half-life (T1/2) of 6 h at 50 °C. EstBASΔSP was immobilized onto a novel epoxy resin (Lx-105s) with a high loading of 96 mg/g. Fourier transform infrared (FTIR) spectroscopy showed that EstBASΔSP was successfully immobilized onto Lx-105s. In addition, immobilization improved its enzymatic performance by widening the tolerable ranges of pH and temperature. The optimum temperature of immobilized EstBASΔSP (Lx-EstBASΔSP) was higher, 60 °C, and overall thermostability improved. T1/2 of Lx-EstBASΔSP and free EstBASΔSP at 60 °C was 105 and 28 min, respectively. Lx-EstBASΔSP was used as a biocatalyst to synthesize chloramphenicol palmitate by regioselective modification at the primary hydroxyl group. Conversion efficiency reached 94.7% at 0.15 M substrate concentration after 24 h. Lx-EstBASΔSP was stable and could be reused for seven cycles, after which it retained over 80% of the original activity.

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Section: Introductionmentioning

confidence: 99%

Immobilization of a Novel ESTBAS Esterase from Bacillus altitudinis onto an Epoxy Resin: Characterization and Regioselective Synthesis of Chloramphenicol Palmitate

et al. 2019

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“…Commercial glucoamylase was not immobilize on glyoxyl agarose, but after chemical amination (the free enzyme retained 80% of its original activity) it could be rapidly immobilized on this support to retain 50% of the activity with improved stability by 500‐fold 69. Multipoint covalent attachment of lipase from Rhizopus oryzae on epoxy‐functionalized silica and silica nanoparticles (MCM‐41 and SBA‐15) cannot be performed at pH 10 due to the low stability of the enzyme 70. Amination of the enzyme with ethylenediamine and carbodiimide (p K =9.2) permitted immobilization at a lower pH value, improving the enzyme stability and selectivity of the enzyme in the hydrolysis of fish oil.…”

Section: Modification Of Proteins To Improve Enzyme Immobilizationmentioning

confidence: 99%

Chemical Modification in the Design of Immobilized Enzyme Biocatalysts: Drawbacks and Opportunities

Rueda

Santos

Ortíz

et al. 2016

The Chemical Record

183

106

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Chemical modification of enzymes and immobilization used to be considered as separate ways to improve enzyme properties. This review shows how the coupled use of both tools may greatly improve the final biocatalyst performance. Chemical modification of a previously immobilized enzyme is far simpler and easier to control than the modification of the free enzyme. Moreover, if protein modification is performed to improve its immobilization (enriching the enzyme in reactive groups), the final features of the immobilized enzyme may be greatly improved. Chemical modification may be directed to improve enzyme stability, but also to improve selectivity, specificity, activity, and even cell penetrability. Coupling of immobilization and chemical modification with site-directed mutagenesis is a powerful instrument to obtain fully controlled modification. Some new ideas such as photoreceptive enzyme modifiers that change their physical properties under UV exposition are discussed.

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“…A técnica de imobilização e o tipo de suporte pode influenciar nas propriedades físico-químicas do biocatalisador, como difusão e eficiência catalítica em cada sistema de reação específico [9,14]. [24] Sepiolite modificada [25] Sílica e nanopartículas de sílica [26] Epóxi [27] Nanopartículas magnéticas [28]…”

Section: Introductionunclassified

Quiz Educativo: Uma Proposta Metodológica Para O Ensino De Tabela Periódica

Silva¹,

Ribeiro²,

Conceição³

et al. 2020

Avanços Das Pesquisas E Inovações Na Engenharia Química 2

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Todo o conteúdo deste livro está licenciado sob uma Licença de Atribuição Creative Commons. Atribuição 4.0 Internacional (CC BY 4.0). O conteúdo dos artigos e seus dados em sua forma, correção e confiabilidade são de responsabilidade exclusiva dos autores. Permitido o download da obra e o compartilhamento desde que sejam atribuídos créditos aos autores, mas sem a possibilidade de alterá-la de nenhuma forma ou utilizá-la para fins comerciais.

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Chemical amination of Rhizopus oryzae lipase for multipoint covalent immobilization on epoxy-functionalized supports: Modulation of stability and selectivity

Cited by 39 publications

References 31 publications

Immobilization of a Novel ESTBAS Esterase from Bacillus altitudinis onto an Epoxy Resin: Characterization and Regioselective Synthesis of Chloramphenicol Palmitate

Immobilization of a Novel ESTBAS Esterase from Bacillus altitudinis onto an Epoxy Resin: Characterization and Regioselective Synthesis of Chloramphenicol Palmitate

Chemical Modification in the Design of Immobilized Enzyme Biocatalysts: Drawbacks and Opportunities

Quiz Educativo: Uma Proposta Metodológica Para O Ensino De Tabela Periódica

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