Production, partial purification and characterization of ligninolytic enzymes from selected basidiomycetes mushroom fungi

In recent years, many research on the quantity of lignocellulosic waste have been developed. The production, partial purification, and characterisation of ligninolytic enzymes from various fungi are described in this work. On the 21st day of incubation in Potato Dextrose (PD) broth, Hypsizygus ulmar...

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Autores principales:	Ramanaiah Illuri, M. Kumar, M. Eyini, V. Veeramanikandan, Khalid S Almaary, Yahya B. Elbadawi, M.A. Biraqdar, P. Balaji
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	Ligninolytic enzymes SDS-PAGE Enzyme purification Enzyme activity Basidiomycete fungus Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/246f7969739b4ca1a5d39184deda6ab0
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spelling	oai:doaj.org-article:246f7969739b4ca1a5d39184deda6ab02021-11-20T04:56:55ZProduction, partial purification and characterization of ligninolytic enzymes from selected basidiomycetes mushroom fungi1319-562X10.1016/j.sjbs.2021.08.026https://doaj.org/article/246f7969739b4ca1a5d39184deda6ab02021-12-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S1319562X21007117https://doaj.org/toc/1319-562XIn recent years, many research on the quantity of lignocellulosic waste have been developed. The production, partial purification, and characterisation of ligninolytic enzymes from various fungi are described in this work. On the 21st day of incubation in Potato Dextrose (PD) broth, Hypsizygus ulmarius developed the most laccase (14.83 × 10−6 IU/ml) and manganese peroxidase (24.11 × 10−6 IU/ml), while Pleurotus florida produced the most lignin peroxidase (19.56 × −6 IU/ml). Laccase (Lac), lignin peroxidase (LiP), and manganese peroxidase (MnP), all generated by selected basidiomycetes mushroom fungi, were largely isolated using ammonium sulphate precipitation followed by dialysis. Laccase, lignin peroxidase, and manganese peroxidase purification findings indicated 1.83, 2.13, and 1.77 fold purity enhancements, respectively. Specific activity of purified laccase enzyme preparations ranged from 305.80 to 376.85 IU/mg, purified lignin peroxidase from 258.51 to 336.95 IU/mg, and purified manganese peroxidase from 253.45 to 529.34 IU/mg. H. ulmarius laccase (376.85 IU/mg) with 1.83 fold purification had the highest specific activity of all the ligninolytic enzymes studied, followed by 2.13 fold purification in lignin peroxidase (350.57 IU/mg) and manganese peroxidase (529.34 IU/mg) with 1.77-fold purification. Three notable bands with molecular weights ranging from 43 to 68 kDa and a single prominent band with a molecular weight of 97.4 kDa were identified on a Native PAGE gel from mycelial proteins of selected mushroom fungus. The SDS PAGE profiles of the mycelial proteins from the selected mushroom fungus were similar to the native PAGE. All three partially purified ligninolytic isozymes display three bands in native gel electrophoresis, with only one prominent band in enzyme activity staining. The 43 kDa, 55 kDa, and 68 kDa protein bands correspond to laccase, lignin peroxidase, and manganese peroxidase, respectively.Ramanaiah IlluriM. KumarM. EyiniV. VeeramanikandanKhalid S AlmaaryYahya B. ElbadawiM.A. BiraqdarP. BalajiElsevierarticleLigninolytic enzymesSDS-PAGEEnzyme purificationEnzyme activityBasidiomycete fungusBiology (General)QH301-705.5ENSaudi Journal of Biological Sciences, Vol 28, Iss 12, Pp 7207-7218 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Ligninolytic enzymes SDS-PAGE Enzyme purification Enzyme activity Basidiomycete fungus Biology (General) QH301-705.5
spellingShingle	Ligninolytic enzymes SDS-PAGE Enzyme purification Enzyme activity Basidiomycete fungus Biology (General) QH301-705.5 Ramanaiah Illuri M. Kumar M. Eyini V. Veeramanikandan Khalid S Almaary Yahya B. Elbadawi M.A. Biraqdar P. Balaji Production, partial purification and characterization of ligninolytic enzymes from selected basidiomycetes mushroom fungi
description	In recent years, many research on the quantity of lignocellulosic waste have been developed. The production, partial purification, and characterisation of ligninolytic enzymes from various fungi are described in this work. On the 21st day of incubation in Potato Dextrose (PD) broth, Hypsizygus ulmarius developed the most laccase (14.83 × 10−6 IU/ml) and manganese peroxidase (24.11 × 10−6 IU/ml), while Pleurotus florida produced the most lignin peroxidase (19.56 × −6 IU/ml). Laccase (Lac), lignin peroxidase (LiP), and manganese peroxidase (MnP), all generated by selected basidiomycetes mushroom fungi, were largely isolated using ammonium sulphate precipitation followed by dialysis. Laccase, lignin peroxidase, and manganese peroxidase purification findings indicated 1.83, 2.13, and 1.77 fold purity enhancements, respectively. Specific activity of purified laccase enzyme preparations ranged from 305.80 to 376.85 IU/mg, purified lignin peroxidase from 258.51 to 336.95 IU/mg, and purified manganese peroxidase from 253.45 to 529.34 IU/mg. H. ulmarius laccase (376.85 IU/mg) with 1.83 fold purification had the highest specific activity of all the ligninolytic enzymes studied, followed by 2.13 fold purification in lignin peroxidase (350.57 IU/mg) and manganese peroxidase (529.34 IU/mg) with 1.77-fold purification. Three notable bands with molecular weights ranging from 43 to 68 kDa and a single prominent band with a molecular weight of 97.4 kDa were identified on a Native PAGE gel from mycelial proteins of selected mushroom fungus. The SDS PAGE profiles of the mycelial proteins from the selected mushroom fungus were similar to the native PAGE. All three partially purified ligninolytic isozymes display three bands in native gel electrophoresis, with only one prominent band in enzyme activity staining. The 43 kDa, 55 kDa, and 68 kDa protein bands correspond to laccase, lignin peroxidase, and manganese peroxidase, respectively.
format	article
author	Ramanaiah Illuri M. Kumar M. Eyini V. Veeramanikandan Khalid S Almaary Yahya B. Elbadawi M.A. Biraqdar P. Balaji
author_facet	Ramanaiah Illuri M. Kumar M. Eyini V. Veeramanikandan Khalid S Almaary Yahya B. Elbadawi M.A. Biraqdar P. Balaji
author_sort	Ramanaiah Illuri
title	Production, partial purification and characterization of ligninolytic enzymes from selected basidiomycetes mushroom fungi
title_short	Production, partial purification and characterization of ligninolytic enzymes from selected basidiomycetes mushroom fungi
title_full	Production, partial purification and characterization of ligninolytic enzymes from selected basidiomycetes mushroom fungi
title_fullStr	Production, partial purification and characterization of ligninolytic enzymes from selected basidiomycetes mushroom fungi
title_full_unstemmed	Production, partial purification and characterization of ligninolytic enzymes from selected basidiomycetes mushroom fungi
title_sort	production, partial purification and characterization of ligninolytic enzymes from selected basidiomycetes mushroom fungi
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/246f7969739b4ca1a5d39184deda6ab0
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Production, partial purification and characterization of ligninolytic enzymes from selected basidiomycetes mushroom fungi

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