Chemical modification of wheat β-amylase by trinitrobenzenesulfonic acid, methoxypolyethylene glycol, and glutaraldehyde to improve its thermal stability and activity

Daba, Tadessa; Kojima, Kenji; Inouye, Kuniyo

doi:10.1016/j.enzmictec.2013.09.006

Cited by 11 publications

(7 citation statements)

References 42 publications

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“…Chemical modification allows for a wider range of chemical groups to enter the enzyme structure and, compared to genetic modification, it does not require prior knowledge of the protein structure, it is fast, and it takes place on the correctly folded enzyme. 1,14,19,[46][47][48] In the present study, native, inactivated, and immobilized lipases were modified with L-proline by means of peptide bonds between the free amino groups of lipases and the carboxyl groups of L-proline, which are activated by the treatment of EDC (Fig. 2).…”

Section: Resultsmentioning

confidence: 95%

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L‐proline modified inactivated lipase and its immobilization on cellulose‐based material: stability and enantioselectivity

Özyılmaz

Çağlar

2021

J of Chemical Tech & Biotech

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BACKGROUND Chemical modification is a simple, low cost, very fast and easy production that has no limits as to the nature of the groups introduced into the enzymes. Chemical modification may be directed to improve enzyme stability, as well as selectivity, specificity, and activity. RESULTS Candida rugosa lipase (CRL) was immobilized onto a cellulose‐based support. The native, inactivated, and immobilized lipases were modified by the reaction of L‐proline (Prl) in the presence of coupling reagent (EDC). The catalytic properties of the modified lipases were evaluated by hydrolysis of p‐nitrophenylpalmitate and the enantioselective hydrolysis of racemic naproxen methyl ester. It was observed that by chemical modification with proline, the hydrolytic activities of native, inactivated, and immobilized lipases increased 2.4, 11.0, and 2.2‐fold, respectively. The immobilized lipase retained 64% of its activity after 120 min at 60 °C, while immobilized L‐proline modified lipase was found to retain 72%. It was also found that the immobilized inactivated lipase kept 44% of its activity at 60 °C for 2 h, while the immobilized L‐proline modified inactivated lipase retained their activity at 65%. In addition, the attained results of the best enantioselectivity of CRL‐Prl exhibited a 2.2‐fold improvement compared to the native enzyme. CONCLUSION The method is simple, cost‐effective, very fast, and it can obtain stronger biocatalysts. It was understood that a lipase lost its activity and could be reused after being simply modified with L‐proline. This study predicts that such facile chemical modifications will open new avenues to develop industrially important biocatalyst with superior catalytic properties. © 2021 Society of Chemical Industry (SCI).

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Section: Resultsmentioning

confidence: 95%

Section: Resultsmentioning

confidence: 99%

L‐proline modified inactivated lipase and its immobilization on cellulose‐based material: stability and enantioselectivity

Özyılmaz

Çağlar

2021

J of Chemical Tech & Biotech

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“…The functional groups such as hydroxyl groups, amino groups, and carboxy group of sericin all have electron donor groups capable to reduce Ag + to Ag ∘ [27][28][29]. The nucleation of nanosilver particle is formed and grown by accumulating with Ag ∘ .…”

Section: In Situ Fabrication and Characterization Of Silver Nanopartimentioning

confidence: 99%

Fabrication and Super-Antibacterial Property of Nanosilver/Sericin/Poly(ethylene oxide) Nanofibers through Electrospinning-Combined Postdeposition Method

Wang

Cui³

et al. 2016

Journal of Nanomaterials

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Nanosilver particle has been used in the nanofiber mats by mixing the nanosilver with the spinning solution for improving the antibacterial property. Although studies have shown that the antibacterial property of nanofiber mats gets increasing, the higher silver content and the larger released resistance of nanosilver from nanofiber mats are obvious. Here, the electrospinning-combined postdeposition method was used to prepare the nanosilver/sericin/poly(ethylene oxide) (Ag/SS/PEO) nanofiber mats and the bacterial reduction rates againstStaphylococcus aureus(S. aureus) andEscherichia coli(E. coli) were analyzed. We found that the Ag/SS/PEO nanofiber mats were excellent antibacterial properties at the lower silver content and the bacterial reduction rates againstS. aureusandE. coliall reached above 99.99%. Our data suggests that the antibacterial property can be improved by introducing the electrospinning-combined postdeposition method.

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“…The results indicated an increase by three times in the catalytic efficiency of the modified phospholipase C, and also higher thermal stability. Daba et al [ 18 ] adopted glutaraldehyde (GA), mPEG chlorotriazine and trinitro-benzene-sulfonic acid (TNBS) to modify β-amylase in malt. The result indicated that mPEG chlorotriazine enhanced the enzymatic activity and thermal stability of β-amylase in malt.…”

Section: Introductionmentioning

confidence: 99%

Chemical Modification of Sweet Potato β-amylase by Mal-mPEG to Improve Its Enzymatic Characteristics

et al. 2018

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The sweet potato β-amylase (SPA) was modified by 6 types of methoxy polyethylene glycol to enhance its specific activity and thermal stability. The aims of the study were to select the optimum modifier, optimize the modification parameters, and further investigate the characterization of the modified SPA. The results showed that methoxy polyethylene glycol maleimide (molecular weight 5000, Mal-mPEG5000) was the optimum modifier of SPA; Under the optimal modification conditions, the specific activity of Mal-mPEG5000-SPA was 24.06% higher than that of the untreated SPA. Mal-mPEG5000-SPA was monomeric with a molecular weight of about 67 kDa by SDS-PAGE. The characteristics of Mal-mPEG5000-SPA were significantly improved. The Km value, Vmax and Ea in Mal-mPEG5000-SPA for sweet potato starch showed that Mal-mPEG5000-SPA had greater affinity for sweet potato starch and higher speed of hydrolysis than SPA. There was no significant difference of the metal ions’ effect on Mal-mPEG5000-SPA and SPA.

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Chemical modification of wheat β-amylase by trinitrobenzenesulfonic acid, methoxypolyethylene glycol, and glutaraldehyde to improve its thermal stability and activity

Cited by 11 publications

References 42 publications

L‐proline modified inactivated lipase and its immobilization on cellulose‐based material: stability and enantioselectivity

L‐proline modified inactivated lipase and its immobilization on cellulose‐based material: stability and enantioselectivity

Fabrication and Super-Antibacterial Property of Nanosilver/Sericin/Poly(ethylene oxide) Nanofibers through Electrospinning-Combined Postdeposition Method

Chemical Modification of Sweet Potato β-amylase by Mal-mPEG to Improve Its Enzymatic Characteristics

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