Characterization of Dimers of Hydroquinone Glucosides Produced by Peroxidase-Catalyzed Polymerization

Kiso, Taro; Shizuma, Motohiro; Watase, Seiji; Kiryu, Takaaki; Murakami, Hiromi; Nakano, Hirofumi

doi:10.1271/bbb.60660

Cited by 6 publications

(2 citation statements)

References 12 publications

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“…Reactions on glycosides or on their aglycones have been performed with other oxidoreductases. Several studies have performed rutin polymerization using different laccases ( 49 – 52 ) and conversions of arbutin with peroxidases ( 53 – 56 ). Arbutin polymerization has also been performed using chemical catalysts ( 57 , 58 ), resulting in enhanced anti-microbial properties.…”

Section: Discussionmentioning

confidence: 99%

Characterization of Amycolatopsis 75iv2 dye-decolorizing peroxidase on O -glycosides

Välimets,

Sun,

Virginia

et al. 2024

Appl Environ Microbiol

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Dye-decolorizing peroxidases are heme peroxidases with a broad range of substrate specificity. Their physiological function is still largely unknown, but a role in the depolymerization of plant cell wall polymers has been widely proposed. Here, a new expression system for bacterial dye-decolorizing peroxidases as well as the activity with previously unexplored plant molecules are reported. The dye-decolorizing peroxidase from Amycolatopsis 75iv2 (DyP2) was heterologously produced in the Gram-positive bacterium Streptomyces lividans TK24 in both intracellular and extracellular forms without external heme supplementation. The enzyme was tested on a series of O -glycosides, which are plant secondary metabolites with a phenyl glycosidic linkage. O -glycosides are of great interest, both for studying the compounds themselves and as potential models for studying specific lignin-carbohydrate complexes. The primary DyP reaction products of salicin, arbutin, fraxin, naringin, rutin, and gossypin were oxidatively coupled oligomers. A cleavage of the glycone moiety upon radical polymerization was observed when using arbutin, fraxin, rutin, and gossypin as substrates. The amount of released glucose from arbutin and fraxin reached 23% and 3% of the total substrate, respectively. The proposed mechanism suggests a destabilization of the ether linkage due to the localization of the radical in the para position. In addition, DyP2 was tested on complex lignocellulosic materials such as wheat straw, spruce, willow, and purified water-soluble lignin fractions, but no remarkable changes in the carbohydrate profile were observed, despite obvious oxidative activity. The exact action of DyP2 on such lignin-carbohydrate complexes therefore remains elusive. IMPORTANCE Peroxidases require correct incorporation of the heme cofactor for activity. Heterologous overproduction of peroxidases often results in an inactive enzyme due to insufficient heme synthesis by the host organism. Therefore, peroxidases are incubated with excess heme during or after purification to reconstitute activity. S. lividans as a production host can produce fully active peroxidases both intracellularly and extracellularly without the need for heme supplementation. This reduces the number of downstream processing steps and is beneficial for more sustainable production of industrially relevant enzymes. Moreover, this research has extended the scope of dye-decolorizing peroxidase applications by studying naturally relevant plant secondary metabolites and analyzing the formed products. A previously overlooked artifact of radical polymerization leading to the release of the glycosyl moiety was revealed, shedding light on the mechanism of DyP peroxidases. The key aspect is the continuous addition, rather than the more common approach of a single addition, of the cosubstrate, hydrogen peroxide. This continuous addition allows the peroxidase to complete a high number of turnovers without self-oxidation.

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Section: Discussionmentioning

confidence: 99%

Characterization of Amycolatopsis 75iv2 dye-decolorizing peroxidase on O -glycosides

Välimets,

Sun,

Virginia

et al. 2024

Appl Environ Microbiol

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“…The structures of the dimers of the two Arbs also supported this conclusion. 14) Accompanying peaks (m z 108n 16 or 108n 32; n, DP of HQ unit) observed in the TOF MS spectra (Fig. 5) may suggest the existence of one or two extra OH groups at one or both terminal units of the phenolic chain.…”

Section: Structures Of Poly (α-Arb) and Poly ( β-Arb) (1) Polymerizamentioning

confidence: 97%

Polymerization of 4-Hydroxyphenyl .ALPHA.-Glucoside and 4-Hydroxyphenyl .BETA.-Glucoside Catalyzed by Horseradish Peroxidase

太郎¹,

基博²,

高明³

et al. 2007

J. Appl. Glycosci.

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Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2007–2008

Harvey

2011

Mass Spectrometry Reviews

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This review is the fifth update of the original review, published in 1999, on the application of MALDI mass spectrometry to the analysis of carbohydrates and glycoconjugates and brings coverage of the literature to the end of 2008. The first section of the review covers fundamental studies, fragmentation of carbohydrate ions, use of derivatives and new software developments for analysis of carbohydrate spectra. Among newer areas of method development are glycan arrays, MALDI imaging and the use of ion mobility spectrometry. The second section of the review discusses applications of MALDI MS to the analysis of different types of carbohydrate. Specific compound classes that are covered include carbohydrate polymers from plants, N- and O-linked glycans from glycoproteins, biopharmaceuticals, glycated proteins, glycolipids, glycosides and various other natural products. There is a short section on the use of MALDI mass spectrometry for the study of enzymes involved in glycan processing and a section on the use of MALDI MS to monitor products of the chemical synthesis of carbohydrates with emphasis on carbohydrate-protein complexes and glycodendrimers. Corresponding analyses by electrospray ionization now appear to outnumber those performed by MALDI and the amount of literature makes a comprehensive review on this technique impractical. However, most of the work relating to sample preparation and glycan synthesis is equally relevant to electrospray and, consequently, those proposing analyses by electrospray should also find material in this review of interest.

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Characterization of Dimers of Hydroquinone Glucosides Produced by Peroxidase-Catalyzed Polymerization

Cited by 6 publications

References 12 publications

Characterization of Amycolatopsis 75iv2 dye-decolorizing peroxidase on O -glycosides

Characterization of Amycolatopsis 75iv2 dye-decolorizing peroxidase on O -glycosides

Polymerization of 4-Hydroxyphenyl .ALPHA.-Glucoside and 4-Hydroxyphenyl .BETA.-Glucoside Catalyzed by Horseradish Peroxidase

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2007–2008

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