Enzymatic synthesis of catechol-functionalized polyphenols with excellent selectivity and productivity

Cheng, Hui; Zou, Yong; Luo, Xiang; Song, Xianheng; Yang, Zhen

doi:10.1016/j.procbio.2018.03.028

Cited by 11 publications

(16 citation statements)

References 40 publications

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“…This reinforces the fact that even when immobilized in the new form (ZIF‐8), the enzyme still holds its strict regioselectivity, quantitatively converting the monophenol to o ‐diphenol as long as the reductant l ‐ascorbic acid is sufficiently supplied. The role of l ‐ascorbic acid as the reductant has been discussed in detail previously 8,9,11 …”

Section: Resultsmentioning

confidence: 99%

“…It should be noted that the latter was achieved by RSM optimization while the current one was not. So far, except our own initial trials, 9,10 no biotechnological approaches have been employed for synthesizing HPS from PS. This study thus offers a new promising biocatalyst for effective synthesis of HPS with a high yield.…”

Section: Resultsmentioning

confidence: 99%

“…7 The synthesis of these catecholic products through regioselective orthohydroxylation on the aromatic ring is always a big challenge to chemists, but can be achieved easily by means of a one-pot enzymatic process using tyrosinase as the catalyst. Our recent studies have demonstrated that cross-linked tyrosinase aggregates (CLEAs) [8][9][10] and tyrosinase-copper phosphate hybrid composites (TCHCs) 11 are both effective catalysts for the synthesis of 3,4-dihydroxyphenylacetic acid, piceatannol, HPS and L-DOPA with excellent selectivity and productivity.…”

Section: Introductionmentioning

confidence: 99%

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Mushroom tyrosinase immobilized in metal–organic frameworks as an excellent catalyst for both catecholic product synthesis and phenolic wastewater treatment

Wei

Feng

et al. 2021

J of Chemical Tech & Biotech

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BACKGROUND Metal–organic frameworks (MOFs) have gained increasing attention with ever‐expanding applications. Developing new MOF‐based immobilized enzymes with new applications is required, not only for demonstrating the generality and applicability of using MOFs for enzyme immobilization, but also to provide potential biocatalysts for industrial applications. To the best of the authors’ knowledge, this is the first report of immobilizing mushroom tyrosinase on zeolitic imidazolate frameworks (ZIFs), with two new applications being developed. RESULTS Upon immobilization through a one‐pot in situ encapsulation approach, the resultant tyrosinase@ZIF‐8 was characterized in structural features and catalytic properties. It was much more stable against pH and temperature relative to the free enzyme. The new biocatalyst was highly efficient in catalyzing the synthesis of catecholic products with pharmacological benefits (l‐DOPA, piceatannol and 3′‐hydroxypterostilbene) and in eliminating phenolic pollutants (phenol, p‐cresol, p‐chlorophenol). Excellent productivities were obtained for the synthesis of the three catecholic products (0.14, 1.38 and 1.46 g L−1 h−1, respectively). A complete removal of the three phenolic pollutants was achieved within 2.5 h, superior to other processes mediated by the same enzyme, or others, immobilized on different supports. The reusability of the new biocatalyst can be remarkably improved by entrapment into polyvinyl alcohol‐alginate gel. CONCLUSIONS Tyrosinase can be immobilized on a new type of MOF with advantages such as easy preparation and excellent catalytic performance. This novel immobilization strategy for tyrosinase offers an excellent biocatalyst potent for both catecholic product synthesis and phenolic wastewater treatment. © 2021 Society of Chemical Industry (SCI).

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Mushroom tyrosinase immobilized in metal–organic frameworks as an excellent catalyst for both catecholic product synthesis and phenolic wastewater treatment

Wei

Feng

et al. 2021

J of Chemical Tech & Biotech

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“…Our previous research has demonstrated that tyrosinase is capable of producing catecholic products such as L-DOPA (Xu et al, 2012), 4-dihydroxyphenylacetic acid (Cheng et al, 2018), piceatannol (Cheng et al, 2018;Wei et al, 2020b), and 3'-hydroxypterostilbene (Cheng et al, 2018;Wei et al, 2020a) from their corresponding monophenol precursors. The rationale behind is the speci c regioselectivity of the enzyme (Scheme 1): It catalyzes the conversion from a monophenol to an o-diphenol (cresolase activity) and subsequently to an o-quinone (catecholase activity); with the aid of a strong reductant such as L-ascorbate, the o-quinone can be reduced back to its o-diphenol form (catecholic product), leaving it as the sole product.…”

Section: Use Of Tyrosinase@hkust-1 As Catalyst For Catecholic Product Synthesismentioning

confidence: 99%

“…Tyrosinase is a copper-containing oxidoreductase catalyzing the hydroxylation of monophenols to o-diphenols and their subsequent oxidation to o-quinones (Robb, 1984). This enzyme has found promising potential in broad applications such as wastewater treatment (Atlow et al, 1984;Xu et al, 2013), biosensor design (Nistor et al, 1999;Wang et al, 2015;Lu et al, 2016), synthesis of pharmaceuticals and nutraceuticals (Pialis et al, 1998;Cheng et al, 2018;Wei et al, 2020b), and prodrug activation for cancer therapy (Lian et al, 2018). Our previous work has demonstrated that this enzyme, when immobilized as cross-linked enzyme aggregates (CLEAs) (Xu et al, 2011), tyrosinase-Cu 3 (PO 4 ) 2 hybrid composites (TCHCs) (Wei et al, 2020b), and tyrosinase@ZIFs (here ZIFs = zeolitic imidazolate frameworks, a type of MOFs) (Wei et al, 2021), had its stability signi cantly enhanced as compared to the free enzyme.…”

Section: Introductionmentioning

confidence: 99%

Tyrosinase@HKUST-1: A Super Stable Biocatalyst Efficient for Catecholic Product Synthesis

Feng

et al. 2021

Preprint

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Although metal-organic frameworks (MOFs) have been considered as promising matrices for enzyme immobilization, HKUST-1, constructed from copper acetate (CuAc2) and benzene 1,3,5-tricarboxylate (BTC), has rarely been explored for this application. In this study, mushroom tyrosinase (EC 1.14.18.1) was immobilized in the form of tyrosinase@HKUST-1 following a simple reaction procedure we developed. The order of mixing BTC with the enzyme prior to addition of CuAc2 is believed to be responsible for the super stability exhibited by the immobilized enzyme so formed. The resultant biocatalyst was characterized in both structural features and catalytic properties. Upon incorporation into the HKUST-1 frameworks, the enzyme gained a prominent enhancement in stability against pH, temperature and storage: When incubated at 50 oC and pH 6.0, tyrosinase@HKUST-1 presented a half-life of 32.6 h, which is 77-fold and over 10-fold higher than that of the free enzyme and its other immobilization forms, respectively; and the catalyst fully maintained its activity for at least 2 months when stored at 30 oC. The applicability of this new biocatalyst was demonstrated by employing it as catalyst for regioselective ortho-hydroxylation reactions to produce catecholic products with huge pharmacological effects, i.e., hydroxytyrosol and L-DOPA, with excellent yields and productivities. This study has thus offered a facile immobilization method to prepare a novel biocatalyst with super stability, and tyrosinase@HKUST-1 so formed from crude mushroom extract provides an efficient catalyst which can be applied to the production of catecholic products with health benefits.

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Tyrosinase from Citreicella sp. as an organophilic enzyme for catechol biosynthesis

Bae,

Lee,

Kim

et al. 2024

Biochemical Engineering Journal

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Enzymatic synthesis of catechol-functionalized polyphenols with excellent selectivity and productivity

Cited by 11 publications

References 40 publications

Mushroom tyrosinase immobilized in metal–organic frameworks as an excellent catalyst for both catecholic product synthesis and phenolic wastewater treatment

Mushroom tyrosinase immobilized in metal–organic frameworks as an excellent catalyst for both catecholic product synthesis and phenolic wastewater treatment

Tyrosinase@HKUST-1: A Super Stable Biocatalyst Efficient for Catecholic Product Synthesis

Tyrosinase from Citreicella sp. as an organophilic enzyme for catechol biosynthesis

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