Tyrosinase immobilized enzyme reactor: Development and evaluation

Oliveira, Karina Bora de; Mischiatti, Keylla Lençone; Fontana, José D.; Oliveira, Brás Heleno de

doi:10.1016/j.jchromb.2013.11.042

Cited by 18 publications

(8 citation statements)

References 25 publications

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“…D, the slope of the linear fitting equation gradually increased with the increasing concentration of kojic acid, but the intercept of the ordinate almost did not change. It could be inferred that kojic acid was a competitive inhibitor for tyrosinase, which was in agreement with the reported literatures .…”

Section: Resultssupporting

confidence: 92%

Screening of tyrosinase inhibitors by capillary electrophoresis with immobilized enzyme microreactor and molecular docking

Cheng

Chen

2016

Electrophoresis

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A new method for screening tyrosinase inhibitors from traditional Chinese medicines (TCMs) was successfully developed by capillary electrophoresis with reliable online immobilized enzyme microreactor (IMER). In addition, molecular docking study has been used for supporting inhibition interaction between enzyme and inhibitors. The IMER of tyrosinase was constructed at the outlet of the capillary by using glutaraldehyde as cross-linker. The parameters including enzyme reaction, separation of the substrate and product, and the performance of immobilized tyrosinase were investigated systematically. Because of using short-end injection procedure, the product and substrate were effectively separated within 2 min. The immobilized tyrosinase could remain 80% active for 30 days at 4°C. The Michaelis-Menten constant of tyrosinase was determined as 1.78 mM. Kojic acid, a known tyrosinase inhibitor, was used as a model compound for the validation of the inhibitors screening method. The half-maximal inhibitory concentration of kojic acid was 5.55 μM. The method was successfully applied for screening tyrosinase inhibitors from 15 compounds of TCM. Four compounds including quercetin, kaempferol, bavachinin, and bakuchiol were found having inhibitory potentials. The results obtained in this work were supported by molecular docking study.

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Section: Resultssupporting

confidence: 92%

Screening of tyrosinase inhibitors by capillary electrophoresis with immobilized enzyme microreactor and molecular docking

Cheng

Chen

2016

Electrophoresis

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“…It is mainly due to the steric hindrance of some active sites caused by the support, which is barely avoided after the enzyme immobilization. 45 From Table S1, † the RI-PMRs also exhibit a lower V max than the free RuBisCO. The reduction of activity is ascribed to the irreversible conformational changes of RuBisCO after immobilization.…”

Section: Kinetic Study Of Ri-pmrsmentioning

confidence: 97%

Biomimetic reusable microfluidic reactors with physically immobilized RuBisCO for glucose precursor production

Zhu

Chen

Tsoi

et al. 2022

Catal. Sci. Technol.

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“…Compared with the kinetic parameters of free RuBisCO, the K m value (the Michaelis–Menten constant) for the RIMRs is relatively higher (0.070 vs. 0.049 mM), inferring a lower affinity of the immobilized enzyme for the reactant. This is a common and intrinsic weakness of immobilized enzymes, owing to the steric hindrance introduced by the coverage of some active site by the support 46 . In addition, the immobilized enzyme may lose the flexibility to bind the natural ligands during catalysis and the diffusion distance for the reactant to the immobilized enzyme on the microchannel sidewalls becomes relatively long (as compared to the free enzyme) 46 .…”

Section: Resultsmentioning

confidence: 99%

“…This is a common and intrinsic weakness of immobilized enzymes, owing to the steric hindrance introduced by the coverage of some active site by the support 46 . In addition, the immobilized enzyme may lose the flexibility to bind the natural ligands during catalysis and the diffusion distance for the reactant to the immobilized enzyme on the microchannel sidewalls becomes relatively long (as compared to the free enzyme) 46 . From Table 1, the RIMRs also exhibited a lower V max (the maximal reaction rate) than that of the free RuBisCO.…”

Section: Resultsmentioning

confidence: 99%

Continuous artificial synthesis of glucose precursor using enzyme-immobilized microfluidic reactors

et al. 2019

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Food production in green crops is severely limited by low activity and poor specificity of D-ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) in natural photosynthesis (NPS). This work presents a scientific solution to overcome this problem by immobilizing RuBisCO into a microfluidic reactor, which demonstrates a continuous production of glucose precursor at 13.8 μmol g −1 RuBisCO min −1 from CO 2 and ribulose-1,5-bisphosphate. Experiments show that the RuBisCO immobilization significantly enhances enzyme stabilities (7.2 folds in storage stability, 6.7 folds in thermal stability), and also improves the reusability (90.4% activity retained after 5 cycles of reuse and 78.5% after 10 cycles). This work mimics the NPS pathway with scalable microreactors for continuous synthesis of glucose precursor using very small amount of RuBisCO. Although still far from industrial production, this work demonstrates artificial synthesis of basic food materials by replicating the light-independent reactions of NPS, which may hold the key to food crisis relief and future space colonization.

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Tyrosinase immobilized enzyme reactor: Development and evaluation

Cited by 18 publications

References 25 publications

Screening of tyrosinase inhibitors by capillary electrophoresis with immobilized enzyme microreactor and molecular docking

Screening of tyrosinase inhibitors by capillary electrophoresis with immobilized enzyme microreactor and molecular docking

Biomimetic reusable microfluidic reactors with physically immobilized RuBisCO for glucose precursor production

Continuous artificial synthesis of glucose precursor using enzyme-immobilized microfluidic reactors

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