Cross-linked enzyme aggregates of Mung bean epoxide hydrolases: A highly active, stable and recyclable biocatalyst for asymmetric hydrolysis of epoxides

Yu, Chunyang; Li, Xiaofeng; Lou, Wen‐Yong; Zong, Min‐Hua

doi:10.1016/j.jbiotec.2013.04.015

Cited by 56 publications

(31 citation statements)

References 31 publications

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“…V max value basically measures how fast the enzyme can hydrolyze a completely saturated substrate; hence an increase in V max after immobilization means that less substrate is needed to be converted to a product per unit of a time. The catalytic efficiency which is denoted by V max /K m of immobilized protease was higher than the catalytic efficiency of ); this is in agreement with Yu et al (2013).…”

Section: Determination Of Kinetic Parameterssupporting

confidence: 88%

“…For higher concentrations of glutaraldehyde, the activity observed was low, this can be explained as an excessive cross-linking happened that resulted in losing some of the flexibility of the enzyme which is required for its activity (Yu et al 2013), or more cross-linking occurred leading to too strong CLEA with a strong diffusion resistance (Dong et al 2010). Usually, the activity of CLEAs prepared using glutaraldehyde appears to be highly dependent on the type of enzyme as well as the concentration of glutaraldehyde.…”

Section: Optimization Of Clea-protease Preparationmentioning

confidence: 99%

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Optimizing the preparation conditions and characterization of a stable and recyclable cross-linked enzyme aggregate (CLEA)-protease

Mahmod

Yusof

Jami

et al. 2016

Bioresour. Bioprocess.

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Background: Cross-linked enzyme aggregate (CLEA) is considered as an effective technique in the production of immobilized biocatalysts for its industrially attractive advantages. Simplicity, stability, low cost, time saving and reusability are proved to be some of CLEA's main advantages. Results:In this study, an active, stable and recyclable CLEA-protease from the viscera of channel catfish Ictalurus punctatus has been prepared. Optimization of the preparation parameters is carried out with the help of Response Surface Methodology. This methodology helped in studying the interaction between the most contributing factors such as cross-linker, precipitant and the additive concentrations. The optimum specific activity for CLEA-protease of 4.512 U/mg protein has shown a high stability against the denaturation forces such as temperature and pH as compared to free protease. It is further found from the study that the highest activity was achieved at the pH of 6.8 and at the temperature of 45 °C. After six cycles, CLEA-protease maintained 28 % of its original activity. Additionally, Michaelis-Menten models were used to determine the kinetic parameters i.e. K m and V max that helped in showing a significant difference after immobilization as compared to free protease. Conclusion:This work found that this novel CLEA-protease can be used as a very active biocatalyst in industrial applications.

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Section: Determination Of Kinetic Parameterssupporting

confidence: 88%

Section: Optimization Of Clea-protease Preparationmentioning

confidence: 99%

Optimizing the preparation conditions and characterization of a stable and recyclable cross-linked enzyme aggregate (CLEA)-protease

Mahmod

Yusof

Jami

et al. 2016

Bioresour. Bioprocess.

View full text Add to dashboard Cite

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“…The higher V max associated with α‐galactosidase CLEAs may be attributed to the highly active enzyme that was obtained after the immobilization procedure. Immobilization sometimes improves the catalytic activity of enzymes despite the common concern of reduced enzyme fexibility, steric hindrance and diffusion limitations …”

Section: Resultsmentioning

confidence: 99%

“…Immobilization sometimes improves the catalytic activity of enzymes despite the common concern of reduced enzyme fexibility, steric hindrance and diffusion limitations. 31,32 wileyonlinelibrary.com/jsfa…”

Section: Kinetic Constantsmentioning

confidence: 99%

Cross‐linked α‐galactosidase aggregates: optimization, characterization and application in the hydrolysis of raffinose‐type oligosaccharides in soymilk

Bayraktar

Önal

2019

J Sci Food Agric

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BACKGROUND Cross‐linked enzyme aggregates (CLEAs) of α‐galactosidase, partially purified from maize (Zea mays) flour, were prepared. The impact of various parameters on enzyme activity was examined to optimize the immobilization procedure. Biochemical characterization of the free and immobilized enzyme was carried out. Stability (thermal, pH, storage and operational stability) and reusability tests were performed. The potential use of the free enzyme and the CLEAs in hydrolysis processes of raffinose‐type oligosaccharides present in soymilk was investigated. RESULTS α‐galactosidase CLEAs were prepared with 47% activity recovery under optimum conditions [1:5 (v/v) enzyme solution:saturated ammonium sulfate solution ratio; 7.5 mg protein and 0.1% (v/v) glutaraldehyde, 6 h, 4 °C, 150 rpm]. α‐galactosidase CLEAs exhibited increased stability in comparison to the free enzyme. The CLEAs and the free enzyme showed a maximum activity at 40°C and their optimal pH values were5.5 and 6.0, respectively. Kinetic constants (KM, Vmax and kcat) were calculated for the free enzyme and the CLEAs in the presence of p‐nitrophenyl‐α‐d‐galactopyranoside, stachyose, melibiose and raffinose. The effect of various chemicals and sugars on enzyme activity showed that both enzyme forms were significantly inhibited by HgCl2 and galactose. The CLEAs hydrolyzed 85% of raffinose and 96% of stachyose. CONCLUSION The α‐galactosidase CLEAs, with their satisfactory enzymatic characteristics, have much potential for use in the food and feed industry. © 2019 Society of Chemical Industry

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“…(R)-PED is a vital synthon for the synthesis of chiral β-adrenergic receptor blockers, antiarrhythmic drugs, and (S)-PED can be employed for the synthesis of production of chiral bisphosphines and the chiral initiator of selective polymerization (Nie et al 2004). In many methods for the synthesis of vicinal diols, epoxide hydrolases are often applied to catalyze the asymmetric hydrolysis of epoxides because of economy and convenience (Yu et al 2013). However, the poor solubility of epoxides in aqueous buffer system is the general issue due to the lipophilic oxiranes (Simeó and Faber 2006).…”

Section: Introductionmentioning

confidence: 99%

The effect of deep eutectic solvents on the asymmetric hydrolysis of styrene oxide by mung bean epoxide hydrolases

Peng

Zhao

et al. 2018

Bioresour. Bioprocess.

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Background: Deep eutectic solvents have attracted considerable attention in numerous fields. There is little information on mung bean epoxide hydrolase-catalyzed epoxides in deep eutectic solvent-containing system. Results:Adding deep eutectic solvents with hydrogen bond donor of acids to phosphate buffer resulted in an obvious decrease in the optical purity of product; nevertheless, the relative slight change was observed by the addition of the deep eutectic solvents with hydrogen bond donor of alcohols and urea. Of the tested deep eutectic solvents, 10% additional amount of choline chloride/trithylene glycol can cause a significant improvement in the enantiopurity of product, from 83.2 ± 1.3% to 87.9 ± 0.3%. Moreover, with the increase in the addition amount of choline chloride/ triethylene glycol from 10 to 30%, the enantiomeric excess of product enhanced from 87.9 to 94%, but a decline of product yield was observed. Finally, the evaluation of enzyme stability showed that the additional amount from 10% to 30% was not beneficial to the activity recovery. Conclusion:In short, adding choline chloride/triethylene glycol contributes to the improvement in the optical purity of (R)-1-phenyl-1, 2-ethanediol in the catalysis of styrene oxide by mung bean epoxide hydrolases; meanwhile, the enzyme immobilization could be essential.

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Cross-linked enzyme aggregates of Mung bean epoxide hydrolases: A highly active, stable and recyclable biocatalyst for asymmetric hydrolysis of epoxides

Cited by 56 publications

References 31 publications

Optimizing the preparation conditions and characterization of a stable and recyclable cross-linked enzyme aggregate (CLEA)-protease

Optimizing the preparation conditions and characterization of a stable and recyclable cross-linked enzyme aggregate (CLEA)-protease

Cross‐linked α‐galactosidase aggregates: optimization, characterization and application in the hydrolysis of raffinose‐type oligosaccharides in soymilk

The effect of deep eutectic solvents on the asymmetric hydrolysis of styrene oxide by mung bean epoxide hydrolases

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