Multi-Enzymatic Synthesis of Lactobionic Acid Using Wood-Degrading Enzymes Produced by White Rot Fungi

Enzymes produced by white rot fungi are involved in the synthesis of secondary metabolites with valuable biotechnological properties. One of these metabolites is lactobionic acid (LBA). The aim of this study was to characterize a novel enzyme system consisting of a cellobiose dehydrogenase from <...

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Main Authors: Wiktoria Piątek-Gołda, Justyna Sulej, Marcin Grąz, Piotr Waśko, Ewa Janik-Zabrotowicz, Monika Osińska-Jaroszuk
Format: Article
Language:English
Published: MDPI AG 2023-03-01
Series:Metabolites
Subjects:
Online Access:https://www.mdpi.com/2218-1989/13/4/469
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author Wiktoria Piątek-Gołda
Justyna Sulej
Marcin Grąz
Piotr Waśko
Ewa Janik-Zabrotowicz
Monika Osińska-Jaroszuk
author_facet Wiktoria Piątek-Gołda
Justyna Sulej
Marcin Grąz
Piotr Waśko
Ewa Janik-Zabrotowicz
Monika Osińska-Jaroszuk
author_sort Wiktoria Piątek-Gołda
collection DOAJ
description Enzymes produced by white rot fungi are involved in the synthesis of secondary metabolites with valuable biotechnological properties. One of these metabolites is lactobionic acid (LBA). The aim of this study was to characterize a novel enzyme system consisting of a cellobiose dehydrogenase from <i>Phlebia lindtneri</i> (PlCDH), a laccase from <i>Cerrena unicolor</i> (CuLAC), a redox mediator (ABTS or DCPIP), and lactose as a substrate. We used quantitative (HPLC) and qualitative methods (TLC, FTIR) to characterise the obtained LBA. The free radical scavenging effect of the synthesised LBA was assessed with the DPPH method. Bactericidal properties were tested against Gram-negative and Gram-positive bacteria. We obtained LBA in all the systems tested; however, the study showed that the temperature of 50 °C with the addition of ABTS was the most advantageous condition for the synthesis of lactobionic acid. A mixture with 13 mM LBA synthesised at 50 °C with DCPIP showed the best antioxidant properties (40% higher compared with the commercial reagent). Furthermore, LBA had an inhibitory effect on all the bacteria tested, but the effect was better against Gram-negative bacteria with growth inhibition no lower than 70%. Summarizing the obtained data, lactobionic acid derived in a multienzymatic system is a compound with great biotechnological potential.
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spelling doaj.art-5e9d7c870e3c4c9c8698e6e8b076ffac2023-11-17T20:23:55ZengMDPI AGMetabolites2218-19892023-03-0113446910.3390/metabo13040469Multi-Enzymatic Synthesis of Lactobionic Acid Using Wood-Degrading Enzymes Produced by White Rot FungiWiktoria Piątek-Gołda0Justyna Sulej1Marcin Grąz2Piotr Waśko3Ewa Janik-Zabrotowicz4Monika Osińska-Jaroszuk5Department of Biochemistry and Biotechnology, Institute of Biological Sciences, Maria Curie-Sklodowska University, 19 Akademicka St., 20-033 Lublin, PolandDepartment of Biochemistry and Biotechnology, Institute of Biological Sciences, Maria Curie-Sklodowska University, 19 Akademicka St., 20-033 Lublin, PolandDepartment of Biochemistry and Biotechnology, Institute of Biological Sciences, Maria Curie-Sklodowska University, 19 Akademicka St., 20-033 Lublin, PolandDepartment of Plant Physiology and Biophysics, Institute of Biological Sciences, Maria Curie-Sklodowska University, 19 Akademicka St., 20-033 Lublin, PolandCore Facility of Biospectroscopy, Institute of Biological Sciences, Maria Curie-Sklodowska University, 19 Akademicka St., 20-033 Lublin, PolandDepartment of Biochemistry and Biotechnology, Institute of Biological Sciences, Maria Curie-Sklodowska University, 19 Akademicka St., 20-033 Lublin, PolandEnzymes produced by white rot fungi are involved in the synthesis of secondary metabolites with valuable biotechnological properties. One of these metabolites is lactobionic acid (LBA). The aim of this study was to characterize a novel enzyme system consisting of a cellobiose dehydrogenase from <i>Phlebia lindtneri</i> (PlCDH), a laccase from <i>Cerrena unicolor</i> (CuLAC), a redox mediator (ABTS or DCPIP), and lactose as a substrate. We used quantitative (HPLC) and qualitative methods (TLC, FTIR) to characterise the obtained LBA. The free radical scavenging effect of the synthesised LBA was assessed with the DPPH method. Bactericidal properties were tested against Gram-negative and Gram-positive bacteria. We obtained LBA in all the systems tested; however, the study showed that the temperature of 50 °C with the addition of ABTS was the most advantageous condition for the synthesis of lactobionic acid. A mixture with 13 mM LBA synthesised at 50 °C with DCPIP showed the best antioxidant properties (40% higher compared with the commercial reagent). Furthermore, LBA had an inhibitory effect on all the bacteria tested, but the effect was better against Gram-negative bacteria with growth inhibition no lower than 70%. Summarizing the obtained data, lactobionic acid derived in a multienzymatic system is a compound with great biotechnological potential.https://www.mdpi.com/2218-1989/13/4/469oxidoreductive enzymeslactobionic acidenzymatic oxidationsecondary metabolite
spellingShingle Wiktoria Piątek-Gołda
Justyna Sulej
Marcin Grąz
Piotr Waśko
Ewa Janik-Zabrotowicz
Monika Osińska-Jaroszuk
Multi-Enzymatic Synthesis of Lactobionic Acid Using Wood-Degrading Enzymes Produced by White Rot Fungi
Metabolites
oxidoreductive enzymes
lactobionic acid
enzymatic oxidation
secondary metabolite
title Multi-Enzymatic Synthesis of Lactobionic Acid Using Wood-Degrading Enzymes Produced by White Rot Fungi
title_full Multi-Enzymatic Synthesis of Lactobionic Acid Using Wood-Degrading Enzymes Produced by White Rot Fungi
title_fullStr Multi-Enzymatic Synthesis of Lactobionic Acid Using Wood-Degrading Enzymes Produced by White Rot Fungi
title_full_unstemmed Multi-Enzymatic Synthesis of Lactobionic Acid Using Wood-Degrading Enzymes Produced by White Rot Fungi
title_short Multi-Enzymatic Synthesis of Lactobionic Acid Using Wood-Degrading Enzymes Produced by White Rot Fungi
title_sort multi enzymatic synthesis of lactobionic acid using wood degrading enzymes produced by white rot fungi
topic oxidoreductive enzymes
lactobionic acid
enzymatic oxidation
secondary metabolite
url https://www.mdpi.com/2218-1989/13/4/469
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