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...
Published in: | Fermentation |
---|---|
Main Authors: | , , , , , , |
Format: | Text |
Language: | English |
Published: |
Multidisciplinary Digital Publishing Institute
2022
|
Subjects: | |
Online Access: | https://doi.org/10.3390/fermentation8110601 |
id |
ftmdpi:oai:mdpi.com:/2311-5637/8/11/601/ |
---|---|
record_format |
openpolar |
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 |
_version_ |
1774712566157672448 |