Temperature and pH Profiling of Extracellular Amylase from Antarctic and Arctic Soil Microfungi

While diversity studies and screening for enzyme activities are important elements of understanding fungal roles in the soil ecosystem, extracting and purifying the target enzyme from the fungal cellular system is also required to characterize the enzyme. This is, in particular, necessary before dev...

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Published in:Fermentation
Main Authors: Abiramy Krishnan, Zazali Alias, Peter Convey, Marcelo González-Aravena, Jerzy Smykla, Mohammed Rizman-Idid, Siti Aisyah Alias
Format: Text
Language:English
Published: Multidisciplinary Digital Publishing Institute 2022
Subjects:
pH
Online Access:https://doi.org/10.3390/fermentation8110601
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spelling ftmdpi:oai:mdpi.com:/2311-5637/8/11/601/ 2023-08-20T04:02:11+02:00 Temperature and pH Profiling of Extracellular Amylase from Antarctic and Arctic Soil Microfungi Abiramy Krishnan Zazali Alias Peter Convey Marcelo González-Aravena Jerzy Smykla Mohammed Rizman-Idid Siti Aisyah Alias agris 2022-11-03 application/pdf https://doi.org/10.3390/fermentation8110601 EN eng Multidisciplinary Digital Publishing Institute Microbial Metabolism, Physiology & Genetics https://dx.doi.org/10.3390/fermentation8110601 https://creativecommons.org/licenses/by/4.0/ Fermentation; Volume 8; Issue 11; Pages: 601 α-amylase enzyme Antarctic Arctic temperature pH Text 2022 ftmdpi https://doi.org/10.3390/fermentation8110601 2023-08-01T07:10:20Z While diversity studies and screening for enzyme activities are important elements of understanding fungal roles in the soil ecosystem, extracting and purifying the target enzyme from the fungal cellular system is also required to characterize the enzyme. This is, in particular, necessary before developing the enzyme for industrial-scale production. In the present study, partially purified α-amylase was obtained from strains of Pseudogymnoascus sp. obtained from Antarctic and Arctic locations. Partially purified α-amylases from these polar fungi exhibited very similar characteristics, including being active at 15 °C, although having a small difference in optimum pH. Both fungal taxa are good candidates for the potential application of cold-active enzymes in biotechnological industries, and further purification and characterization steps are now required. The α-amylases from polar fungi are attractive in terms of industrial development because they are active at lower temperatures and acidic pH, thus potentially creating energy and cost savings. Furthermore, they prevent the production of maltulose, which is an undesirable by-product often formed under alkaline conditions. Psychrophilic amylases from the polar Pseudogymnoascus sp. investigated in the present study could provide a valuable future contribution to biotechnological applications. Text Antarc* Antarctic Arctic MDPI Open Access Publishing Antarctic Arctic Fermentation 8 11 601
institution Open Polar
collection MDPI Open Access Publishing
op_collection_id ftmdpi
language English
topic α-amylase
enzyme
Antarctic
Arctic
temperature
pH
spellingShingle α-amylase
enzyme
Antarctic
Arctic
temperature
pH
Abiramy Krishnan
Zazali Alias
Peter Convey
Marcelo González-Aravena
Jerzy Smykla
Mohammed Rizman-Idid
Siti Aisyah Alias
Temperature and pH Profiling of Extracellular Amylase from Antarctic and Arctic Soil Microfungi
topic_facet α-amylase
enzyme
Antarctic
Arctic
temperature
pH
description While diversity studies and screening for enzyme activities are important elements of understanding fungal roles in the soil ecosystem, extracting and purifying the target enzyme from the fungal cellular system is also required to characterize the enzyme. This is, in particular, necessary before developing the enzyme for industrial-scale production. In the present study, partially purified α-amylase was obtained from strains of Pseudogymnoascus sp. obtained from Antarctic and Arctic locations. Partially purified α-amylases from these polar fungi exhibited very similar characteristics, including being active at 15 °C, although having a small difference in optimum pH. Both fungal taxa are good candidates for the potential application of cold-active enzymes in biotechnological industries, and further purification and characterization steps are now required. The α-amylases from polar fungi are attractive in terms of industrial development because they are active at lower temperatures and acidic pH, thus potentially creating energy and cost savings. Furthermore, they prevent the production of maltulose, which is an undesirable by-product often formed under alkaline conditions. Psychrophilic amylases from the polar Pseudogymnoascus sp. investigated in the present study could provide a valuable future contribution to biotechnological applications.
format Text
author Abiramy Krishnan
Zazali Alias
Peter Convey
Marcelo González-Aravena
Jerzy Smykla
Mohammed Rizman-Idid
Siti Aisyah Alias
author_facet Abiramy Krishnan
Zazali Alias
Peter Convey
Marcelo González-Aravena
Jerzy Smykla
Mohammed Rizman-Idid
Siti Aisyah Alias
author_sort Abiramy Krishnan
title Temperature and pH Profiling of Extracellular Amylase from Antarctic and Arctic Soil Microfungi
title_short Temperature and pH Profiling of Extracellular Amylase from Antarctic and Arctic Soil Microfungi
title_full Temperature and pH Profiling of Extracellular Amylase from Antarctic and Arctic Soil Microfungi
title_fullStr Temperature and pH Profiling of Extracellular Amylase from Antarctic and Arctic Soil Microfungi
title_full_unstemmed Temperature and pH Profiling of Extracellular Amylase from Antarctic and Arctic Soil Microfungi
title_sort temperature and ph profiling of extracellular amylase from antarctic and arctic soil microfungi
publisher Multidisciplinary Digital Publishing Institute
publishDate 2022
url https://doi.org/10.3390/fermentation8110601
op_coverage agris
geographic Antarctic
Arctic
geographic_facet Antarctic
Arctic
genre Antarc*
Antarctic
Arctic
genre_facet Antarc*
Antarctic
Arctic
op_source Fermentation; Volume 8; Issue 11; Pages: 601
op_relation Microbial Metabolism, Physiology & Genetics
https://dx.doi.org/10.3390/fermentation8110601
op_rights https://creativecommons.org/licenses/by/4.0/
op_doi https://doi.org/10.3390/fermentation8110601
container_title Fermentation
container_volume 8
container_issue 11
container_start_page 601
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