Peroxidase-catalyzed generation of catechin oligomers that inhibit glucosyltransferase from<i>Streptococcus sobrinus</i>

Hamada, Shigeyuki; Kontani, Masanori; Hosono, Hidekazu; Ono, Hiroyuki; Tanaka, Takaharu; Ooshima, Takashi; Mitsunaga, Tohru; Abe, Isao

doi:10.1111/j.1574-6968.1996.tb08458.x

Cited by 48 publications

(14 citation statements)

References 15 publications

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“…Numerous biological activities have been reported for green tea and its contents, among them, the preventive effects against cancer are most notable. Peroxidase catalyzed the oxidative polymerization of catechin to produce the oligomer with a degree of polymerization less than 5 . Kinetic study on the oxidation of catechin by peroxidase from strawberries showed highly efficient catalytic activity of the enzyme at low concentration of hydrogen peroxide. , The reaction products obtained by the HRP catalyst were analyzed by reversed-phase and size-exclusion chromatographies. , The products obtained by using HRP and polyphenol oxidase as catalysts were comparably studied.…”

Section: Oxidoreductasesmentioning

confidence: 99%

Enzymes as Green Catalysts for Precision Macromolecular Synthesis

et al. 2016

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The present article comprehensively reviews the macromolecular synthesis using enzymes as catalysts. Among the six main classes of enzymes, the three classes, oxidoreductases, transferases, and hydrolases, have been employed as catalysts for the in vitro macromolecular synthesis and modification reactions. Appropriate design of reaction including monomer and enzyme catalyst produces macromolecules with precisely controlled structure, similarly as in vivo enzymatic reactions. The reaction controls the product structure with respect to substrate selectivity, chemo-selectivity, regio-selectivity, stereoselectivity, and choro-selectivity. Oxidoreductases catalyze various oxidation polymerizations of aromatic compounds as well as vinyl polymerizations. Transferases are effective catalysts for producing polysaccharide having a variety of structure and polyesters. Hydrolases catalyzing the bond-cleaving of macromolecules in vivo, catalyze the reverse reaction for bond forming in vitro to give various polysaccharides and functionalized polyesters. The enzymatic polymerizations allowed the first in vitro synthesis of natural polysaccharides having complicated structures like cellulose, amylose, xylan, chitin, hyaluronan, and chondroitin. These polymerizations are "green" with several respects; nontoxicity of enzyme, high catalyst efficiency, selective reactions under mild conditions using green solvents and renewable starting materials, and producing minimal byproducts. Thus, the enzymatic polymerization is desirable for the environment and contributes to "green polymer chemistry" for maintaining sustainable society.

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Section: Oxidoreductasesmentioning

confidence: 99%

Enzymes as Green Catalysts for Precision Macromolecular Synthesis

et al. 2016

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“…The pathogenicity is closely related to the production of extracellular, water insoluble glucans from sucrose by glucosyltransferase and acid release from various fermentable sugars. Poly(catechin) obtained using HRP catalyst in a phosphate buffer (pH ¼ 6) markedly inhibited glucosyltransferase from Streptococcus sorbrinus 6715, [48] whereas the inhibitory effect of catechin for this enzyme was very low.…”

Section: Enzymatically Polymerized Flavonoidsmentioning

confidence: 99%

Artificial Polymeric Flavonoids: Synthesis and Applications

Uyama

2007

Macromolecular Bioscience

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Flavonoids, one of the most numerous and best studied groups of plant polyphenols, are well known to exhibit various biological and pharmacological effects. Functional artificial polymeric flavonoids, flavonoid polymers and amine containing polymer-flavonoid conjugates have been developed. The acid-catalyzed polymerization of catechin and aldehydes proceeds regioselectively to produce catechin-aldehyde polycondensates. Peroxidases and laccases catalyze the oxidative coupling of flavonoids and oxidative conjugation with polyamines. The resulting polymers show much higher antioxidant activities than the flavonoid monomers. In addition, these polymeric flavonoids efficiently inhibit disease related enzymes, such as xanthine oxidase, collagenase, elastase, hyaluronidase and tyrosinase. Based on these results, the molecular design for amplification of the biological and pharmacological properties of flavonoids is proposed.

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“…Another enzyme utilized in the polymerization of flavonoids is horseradish peroxidase (HRP). As a result of the reaction with horseradish peroxidase, the polymeric structures of catechin [12,13,26] and quercetin [27] were synthesized. The enzymatic reactions of polyphenols influenced their biological activity.…”

Section: Introductionmentioning

confidence: 99%

Polymeric Forms of Plant Flavonoids Obtained by Enzymatic Reactions

2022

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Naringenin is one of the flavonoids originating from citrus fruit. This polyphenol is mainly found in grapefruit, orange and lemon. The antioxidant and antimicrobial properties of flavonoids depend on their structure, including the polymeric form. The aim of this research was to achieve enzymatic polymerization of naringenin and to study the properties of poly(naringenin). The polymerization was performed by methods using two different enzymes, i.e., laccase and horseradish peroxidase (HRP). According to the literature data, naringenin had not been polymerized previously using the enzymatic polymerization method. Therefore, obtaining polymeric naringenin by reaction with enzymes is a scientific novelty. The research methodology included analysis of the structure of poly(naringenin) by NMR, GPC, FTIR and UV-Vis and its morphology by SEM, as well as analysis of its properties, i.e., thermal stability (DSC and TGA), antioxidant activity (ABTS, DPPH, FRAP and CUPRAC) and antimicrobial properties. Naringenin oligomers were obtained as a result of polymerization with two types of enzymes. The polymeric forms of naringenin were more resistant to thermo-oxidation; the final oxidation temperature To of naringenin catalyzed by laccase (poly(naringenin)-laccase) was 28.2 °C higher, and poly(naringenin)-HRP 23.6 °C higher than that of the basic flavonoid. Additionally, due to the higher molar mass and associated increase in OH groups in the structure, naringenin catalyzed by laccase (poly(naringenin)-laccase) showed better activity for scavenging ABTS+• radicals than naringenin catalyzed by HRP (poly(naringenin)-HRP) and naringenin. In addition, poly(naringenin)-laccase at a concentration of 5 mg/mL exhibited better microbial activity against E. coli than monomeric naringenin.

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Peroxidase-catalyzed generation of catechin oligomers that inhibit glucosyltransferase fromStreptococcus sobrinus

Cited by 48 publications

References 15 publications

Enzymes as Green Catalysts for Precision Macromolecular Synthesis

Enzymes as Green Catalysts for Precision Macromolecular Synthesis

Artificial Polymeric Flavonoids: Synthesis and Applications

Polymeric Forms of Plant Flavonoids Obtained by Enzymatic Reactions

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