Bioprospecting of the agaricomycete Ganoderma australe GPC191 as novel source for l-asparaginase production

Abstract l-Asparaginase is a therapeutically and industrially-competent enzyme, acting predominantly as an anti-neoplastic and anti-cancerous agent. The existing formulations of prokaryotic l-asparaginase are often toxic and contain l-glutaminase and urease residues, thereby increasing the purificat...

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Main Authors: Meghna Chakraborty, Srividya Shivakumar
Format: Article
Language:English
Published: Nature Publishing Group 2021-03-01
Series:Scientific Reports
Online Access:https://doi.org/10.1038/s41598-021-84949-5
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spelling doaj-aef4624166fe4676ac5228a6aeb407ea2021-03-21T12:38:16ZengNature Publishing GroupScientific Reports2045-23222021-03-011111810.1038/s41598-021-84949-5Bioprospecting of the agaricomycete Ganoderma australe GPC191 as novel source for l-asparaginase productionMeghna Chakraborty0Srividya Shivakumar1Department of Microbiology, School of Sciences, Block-1, JAIN (Deemed To-Be University)Department of Microbiology, School of Sciences, Block-1, JAIN (Deemed To-Be University)Abstract l-Asparaginase is a therapeutically and industrially-competent enzyme, acting predominantly as an anti-neoplastic and anti-cancerous agent. The existing formulations of prokaryotic l-asparaginase are often toxic and contain l-glutaminase and urease residues, thereby increasing the purification steps. Production of l-glutaminase and urease free l-asparaginase is thus desired. In this research, bioprospecting of isolates from the less explored class Agaricomycetes was undertaken for l-asparaginase production. Plate assay (using phenol red and bromothymol blue dyes) was performed followed by estimation of l-asparaginase, l-glutaminase and urease activities by Nesslerization reaction for all the isolates. The isolate displaying the desired enzyme production was subjected to morphological, molecular identification, and phylogenetic analysis with statistical validation using Jukes-Cantor by Neighbour-joining tree of Maximum Likelihood statistical method. Among the isolates, Ganoderma australe GPC191 with significantly high zone index value (5.581 ± 0.045 at 120 h) and enzyme activity (1.57 ± 0.006 U/mL), devoid of l-glutaminase and urease activity was selected. The present study for the first-time reported G. australe as the potential source of l-glutaminase and urease-free l-asparaginase and also is one of the few studies contributing to the literature of G. australe in India. Hence, it can be postulated that it may find its future application in pharmaceutical and food industries.https://doi.org/10.1038/s41598-021-84949-5
collection DOAJ
language English
format Article
sources DOAJ
author Meghna Chakraborty
Srividya Shivakumar
spellingShingle Meghna Chakraborty
Srividya Shivakumar
Bioprospecting of the agaricomycete Ganoderma australe GPC191 as novel source for l-asparaginase production
Scientific Reports
author_facet Meghna Chakraborty
Srividya Shivakumar
author_sort Meghna Chakraborty
title Bioprospecting of the agaricomycete Ganoderma australe GPC191 as novel source for l-asparaginase production
title_short Bioprospecting of the agaricomycete Ganoderma australe GPC191 as novel source for l-asparaginase production
title_full Bioprospecting of the agaricomycete Ganoderma australe GPC191 as novel source for l-asparaginase production
title_fullStr Bioprospecting of the agaricomycete Ganoderma australe GPC191 as novel source for l-asparaginase production
title_full_unstemmed Bioprospecting of the agaricomycete Ganoderma australe GPC191 as novel source for l-asparaginase production
title_sort bioprospecting of the agaricomycete ganoderma australe gpc191 as novel source for l-asparaginase production
publisher Nature Publishing Group
series Scientific Reports
issn 2045-2322
publishDate 2021-03-01
description Abstract l-Asparaginase is a therapeutically and industrially-competent enzyme, acting predominantly as an anti-neoplastic and anti-cancerous agent. The existing formulations of prokaryotic l-asparaginase are often toxic and contain l-glutaminase and urease residues, thereby increasing the purification steps. Production of l-glutaminase and urease free l-asparaginase is thus desired. In this research, bioprospecting of isolates from the less explored class Agaricomycetes was undertaken for l-asparaginase production. Plate assay (using phenol red and bromothymol blue dyes) was performed followed by estimation of l-asparaginase, l-glutaminase and urease activities by Nesslerization reaction for all the isolates. The isolate displaying the desired enzyme production was subjected to morphological, molecular identification, and phylogenetic analysis with statistical validation using Jukes-Cantor by Neighbour-joining tree of Maximum Likelihood statistical method. Among the isolates, Ganoderma australe GPC191 with significantly high zone index value (5.581 ± 0.045 at 120 h) and enzyme activity (1.57 ± 0.006 U/mL), devoid of l-glutaminase and urease activity was selected. The present study for the first-time reported G. australe as the potential source of l-glutaminase and urease-free l-asparaginase and also is one of the few studies contributing to the literature of G. australe in India. Hence, it can be postulated that it may find its future application in pharmaceutical and food industries.
url https://doi.org/10.1038/s41598-021-84949-5
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AT srividyashivakumar bioprospectingoftheagaricomyceteganodermaaustralegpc191asnovelsourceforlasparaginaseproduction
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