Enhanced Thermostability of a Fungal Alkaline Protease by Different Additives

A fungal strain (Conidiobolus brefeldianus MTCC 5184) isolated from plant detritus secreted a high activity alkaline protease. Thermostability studies of the fungal alkaline protease (FAP) revealed that the protease is stable up to 50°C with 40% residual activity after one hour. Effect of various ad...

Descripción completa

Detalles Bibliográficos
Autores principales: Nirmal, Nilesh P., Laxman, R. Seeta
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4106064/
https://www.ncbi.nlm.nih.gov/pubmed/25105022
http://dx.doi.org/10.1155/2014/109303
_version_ 1782327466627432448
author Nirmal, Nilesh P.
Laxman, R. Seeta
author_facet Nirmal, Nilesh P.
Laxman, R. Seeta
author_sort Nirmal, Nilesh P.
collection PubMed
description A fungal strain (Conidiobolus brefeldianus MTCC 5184) isolated from plant detritus secreted a high activity alkaline protease. Thermostability studies of the fungal alkaline protease (FAP) revealed that the protease is stable up to 50°C with 40% residual activity after one hour. Effect of various additives such as sugars, sugar alcohols, polyols, and salts, on the thermostability of FAP was evaluated. Among the additives tested, glycerol, mannitol, xylitol, sorbitol, and trehalose were found to be very effective in increasing the stability of FAP, which was found to be concentration dependent. Fivefold increase in residual activity of FAP was observed in the presence of trehalose (50%) and sorbitol (50%) at 50°C for 4 h, compared to FAP without additive. Other additives like calcium at 20 mM and 10–15% ammonium sulphate showed lower stability improvement than trehalose and sorbitol. NaCl, MgCl(2), K(2)HPO(4), and glycine were found to be poor stabilizers and showed only a marginal improvement. PEG 6000 did not show any increase in stability but was found to be slightly inhibitory.
format Online
Article
Text
id pubmed-4106064
institution National Center for Biotechnology Information
language English
publishDate 2014
publisher Hindawi Publishing Corporation
record_format MEDLINE/PubMed
spelling pubmed-41060642014-08-07 Enhanced Thermostability of a Fungal Alkaline Protease by Different Additives Nirmal, Nilesh P. Laxman, R. Seeta Enzyme Res Research Article A fungal strain (Conidiobolus brefeldianus MTCC 5184) isolated from plant detritus secreted a high activity alkaline protease. Thermostability studies of the fungal alkaline protease (FAP) revealed that the protease is stable up to 50°C with 40% residual activity after one hour. Effect of various additives such as sugars, sugar alcohols, polyols, and salts, on the thermostability of FAP was evaluated. Among the additives tested, glycerol, mannitol, xylitol, sorbitol, and trehalose were found to be very effective in increasing the stability of FAP, which was found to be concentration dependent. Fivefold increase in residual activity of FAP was observed in the presence of trehalose (50%) and sorbitol (50%) at 50°C for 4 h, compared to FAP without additive. Other additives like calcium at 20 mM and 10–15% ammonium sulphate showed lower stability improvement than trehalose and sorbitol. NaCl, MgCl(2), K(2)HPO(4), and glycine were found to be poor stabilizers and showed only a marginal improvement. PEG 6000 did not show any increase in stability but was found to be slightly inhibitory. Hindawi Publishing Corporation 2014 2014-07-03 /pmc/articles/PMC4106064/ /pubmed/25105022 http://dx.doi.org/10.1155/2014/109303 Text en Copyright © 2014 N. P. Nirmal and R. S. Laxman. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Nirmal, Nilesh P.
Laxman, R. Seeta
Enhanced Thermostability of a Fungal Alkaline Protease by Different Additives
title Enhanced Thermostability of a Fungal Alkaline Protease by Different Additives
title_full Enhanced Thermostability of a Fungal Alkaline Protease by Different Additives
title_fullStr Enhanced Thermostability of a Fungal Alkaline Protease by Different Additives
title_full_unstemmed Enhanced Thermostability of a Fungal Alkaline Protease by Different Additives
title_short Enhanced Thermostability of a Fungal Alkaline Protease by Different Additives
title_sort enhanced thermostability of a fungal alkaline protease by different additives
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4106064/
https://www.ncbi.nlm.nih.gov/pubmed/25105022
http://dx.doi.org/10.1155/2014/109303
work_keys_str_mv AT nirmalnileshp enhancedthermostabilityofafungalalkalineproteasebydifferentadditives
AT laxmanrseeta enhancedthermostabilityofafungalalkalineproteasebydifferentadditives