Literature DB >> 27687230

Degradation and polymerization of monolignols by Abortiporus biennis, and induction of its degradation with a reducing agent.

Chang-Young Hong1, Se-Yeong Park1, Seon-Hong Kim1, Su-Yeon Lee2, Won-Sil Choi3, In-Gyu Choi4,5,6.   

Abstract

This study was carried out to better understand the characteristic modification mechanisms of monolignols by enzyme system of Abortiporus biennis and to induce the degradation of monolignols. Degradation and polymerization of monolignols were simultaneously induced by A. biennis. Whole cells of A. biennis degraded coniferyl alcohol to vanillin and coniferyl aldehyde, and degraded sinapyl alcohol to 2,6-dimethoxybenzene- 1,4-diol, with the production of dimers. The molecular weight of monolignols treated with A. biennis increased drastically. The activities of lignin degrading enzymes were monitored for 24 h to determine whether there was any correlation between monolignol biomodification and ligninolytic enzymes. We concluded that complex enzyme systems were involved in the degradation and polymerization of monolignols. To degrade monolignols, ascorbic acid was added to the culture medium as a reducing agent. In the presence of ascorbic acid, the molecular weight was less increased in the case of coniferyl alcohol, while that of sinapyl alcohol was similar to that of the control. Furthermore, the addition of ascorbic acid led to the production of various degraded compounds: syringaldehyde and acid compounds. Accordingly, these results demonstrated that ascorbic acid prevented the rapid polymerization of monolignols, thus stabilizing radicals generated by enzymes of A. biennis. Thereafter, A. biennis catalyzed the oxidation of stable monolignols. As a result, ascorbic acid facilitated predominantly monolignols degradation by A. biennis through the stabilization of radicals. These findings showed outstanding ability of A. biennis to modify the lignin compounds rapidly and usefully.

Entities:  

Keywords:  Abortiporus biennis; degradation; monolignols; polymerization; reducing agent; white rot basidiomycetes

Mesh:

Substances:

Year:  2016        PMID: 27687230     DOI: 10.1007/s12275-016-6158-9

Source DB:  PubMed          Journal:  J Microbiol        ISSN: 1225-8873            Impact factor:   3.422


  23 in total

1.  Laccases: structure, reactions, distribution.

Authors:  Harald Claus
Journal:  Micron       Date:  2004       Impact factor: 2.251

2.  Insight into functional diversity of cytochrome P450 in the white-rot basidiomycete Phanerochaete chrysosporium: involvement of versatile monooxygenase.

Authors:  Shinji Hirosue; Masahiro Tazaki; Nobuhiro Hiratsuka; Satoshi Yanai; Hiroki Kabumoto; Raku Shinkyo; Akira Arisawa; Toshiyuki Sakaki; Hiroshi Tsunekawa; Osamu Johdo; Hirofumi Ichinose; Hiroyuki Wariishi
Journal:  Biochem Biophys Res Commun       Date:  2011-03-21       Impact factor: 3.575

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Authors:  C Rüttimann-Johnson; R T Lamar
Journal:  Appl Environ Microbiol       Date:  1996-10       Impact factor: 4.792

Review 4.  Can laccases catalyze bond cleavage in lignin?

Authors:  Line Munk; Anna K Sitarz; Dayanand C Kalyani; J Dalgaard Mikkelsen; Anne S Meyer
Journal:  Biotechnol Adv       Date:  2015-01-03       Impact factor: 14.227

5.  Polymerization of guaiacol by lignin-degrading manganese peroxidase from Bjerkandera adusta in aqueous organic solvents.

Authors:  K Iwahara; Y Honda; T Watanabe; M Kuwahara
Journal:  Appl Microbiol Biotechnol       Date:  2000-07       Impact factor: 4.813

6.  Polymerization of lignosulfonates by the laccase-HBT (1-hydroxybenzotriazole) system improves dispersibility.

Authors:  Endry Nugroho Prasetyo; Tukayi Kudanga; Lars Østergaard; Jorge Rencoret; Ana Gutiérrez; José C del Río; J Ignacio Santos; Lidia Nieto; Jesús Jiménez-Barbero; Angel T Martínez; Jiebing Li; Göran Gellerstedt; Stéphane Lepifre; Carla Silva; Su Yeon Kim; Artur Cavaco-Paulo; Bente Seljebakken Klausen; Bjart Frode Lutnaes; Gibson S Nyanhongo; Georg M Guebitz
Journal:  Bioresour Technol       Date:  2010-02-21       Impact factor: 9.642

7.  Polymerization of monolignols by redox shuttle-mediated enzymatic oxidation: a new model in lignin biosynthesis I.

Authors:  Hans Onnerud; Liming Zhang; Göran Gellerstedt; Gunnar Henriksson
Journal:  Plant Cell       Date:  2002-08       Impact factor: 11.277

Review 8.  Structure and action mechanism of ligninolytic enzymes.

Authors:  Dominic W S Wong
Journal:  Appl Biochem Biotechnol       Date:  2008-06-26       Impact factor: 2.926

9.  Aromatic ring cleavage of 4,6-di(tert-butyl)guaiacol, a phenolic lignin model compound, by laccase of Coriolus versicolor.

Authors:  S Kawai; T Umezawa; M Shimada; T Higuchi
Journal:  FEBS Lett       Date:  1988-08-29       Impact factor: 4.124

10.  Polymerisation of Kraft lignin from black liquors by laccase from Myceliophthora thermophila: effect of operational conditions and black liquor origin.

Authors:  S Gouveia; C Fernández-Costas; M A Sanromán; D Moldes
Journal:  Bioresour Technol       Date:  2013-01-03       Impact factor: 9.642

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