Discovery of cold-active protease from psychrophilic bacteria isolated from Antarctic region for bio-prospecting
The Antarctic region is a new frontier as natural sources for bio-prospecting purposes. Its extreme cold temperature may provide unique enzyme characteristics that have valuable potential for industrial and biotechnological applications. This study was designed to discover proteases that are activ...
| Main Authors: | , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Penerbit Universiti Kebangsaan Malaysia
2020
|
| Online Access: | http://journalarticle.ukm.my/15699/ http://journalarticle.ukm.my/15699/1/49_01_06.pdf |
| _version_ | 1848813862986448896 |
|---|---|
| author | Muhammad Asyraf Abd Latip, Siti Aisyah Alias, Smykla, Jerzy Faridah Yusof, Mohd Azrul Naim Mohamad, Noor Faizul Hadry Nordin, |
| author_facet | Muhammad Asyraf Abd Latip, Siti Aisyah Alias, Smykla, Jerzy Faridah Yusof, Mohd Azrul Naim Mohamad, Noor Faizul Hadry Nordin, |
| author_sort | Muhammad Asyraf Abd Latip, |
| building | UKM Institutional Repository |
| collection | Online Access |
| description | The Antarctic region is a new frontier as natural sources for bio-prospecting purposes. Its extreme cold temperature may
provide unique enzyme characteristics that have valuable potential for industrial and biotechnological applications. This study
was designed to discover proteases that are activate and can work at very low temperatures. Soil samples from the Antarctic
region were screened for protease activity on skim milk agar at 4°C. Bacteria that showed clear halo zone around the colonies
were selected and identified through 16S rDNA sequencing. Out of 35 bacteria, 10 bacteria that showed rapid halo zone
formation were selected and further analyzed by enzymatic assay. By using azocasein as a substrate, the reaction was measured
using spectrophotometer at OD340 nm. Based on the 16S rDNA sequence, phylogenetic analysis showed that 88% of the
bacteria producing protease were from Pseudomonas sp., 9% from Arthrobacter sp. and 3% from Paenibacillus sp. For
enzymatic assay analysis, sample SC8 showed the highest protease activity compared to other 10 samples. This preliminary
study successfully demonstrated cold active protease producers that can be further investigated for bioprospecting. In future,
purification and characterization of this enzyme is required in order to optimize the enzyme activity. |
| first_indexed | 2025-11-15T00:24:56Z |
| format | Article |
| id | oai:generic.eprints.org:15699 |
| institution | Universiti Kebangasaan Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T00:24:56Z |
| publishDate | 2020 |
| publisher | Penerbit Universiti Kebangsaan Malaysia |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | oai:generic.eprints.org:156992020-11-16T23:35:27Z http://journalarticle.ukm.my/15699/ Discovery of cold-active protease from psychrophilic bacteria isolated from Antarctic region for bio-prospecting Muhammad Asyraf Abd Latip, Siti Aisyah Alias, Smykla, Jerzy Faridah Yusof, Mohd Azrul Naim Mohamad, Noor Faizul Hadry Nordin, The Antarctic region is a new frontier as natural sources for bio-prospecting purposes. Its extreme cold temperature may provide unique enzyme characteristics that have valuable potential for industrial and biotechnological applications. This study was designed to discover proteases that are activate and can work at very low temperatures. Soil samples from the Antarctic region were screened for protease activity on skim milk agar at 4°C. Bacteria that showed clear halo zone around the colonies were selected and identified through 16S rDNA sequencing. Out of 35 bacteria, 10 bacteria that showed rapid halo zone formation were selected and further analyzed by enzymatic assay. By using azocasein as a substrate, the reaction was measured using spectrophotometer at OD340 nm. Based on the 16S rDNA sequence, phylogenetic analysis showed that 88% of the bacteria producing protease were from Pseudomonas sp., 9% from Arthrobacter sp. and 3% from Paenibacillus sp. For enzymatic assay analysis, sample SC8 showed the highest protease activity compared to other 10 samples. This preliminary study successfully demonstrated cold active protease producers that can be further investigated for bioprospecting. In future, purification and characterization of this enzyme is required in order to optimize the enzyme activity. Penerbit Universiti Kebangsaan Malaysia 2020 Article PeerReviewed application/pdf en http://journalarticle.ukm.my/15699/1/49_01_06.pdf Muhammad Asyraf Abd Latip, and Siti Aisyah Alias, and Smykla, Jerzy and Faridah Yusof, and Mohd Azrul Naim Mohamad, and Noor Faizul Hadry Nordin, (2020) Discovery of cold-active protease from psychrophilic bacteria isolated from Antarctic region for bio-prospecting. Malaysian Applied Biology, 49 (1). pp. 55-60. ISSN 0126-8643 http://www.mabjournal.com/index.php?option=com_content&view=article&id=981&catid=59:current-view&Itemid=56 |
| spellingShingle | Muhammad Asyraf Abd Latip, Siti Aisyah Alias, Smykla, Jerzy Faridah Yusof, Mohd Azrul Naim Mohamad, Noor Faizul Hadry Nordin, Discovery of cold-active protease from psychrophilic bacteria isolated from Antarctic region for bio-prospecting |
| title | Discovery of cold-active protease from psychrophilic bacteria isolated from Antarctic region for bio-prospecting |
| title_full | Discovery of cold-active protease from psychrophilic bacteria isolated from Antarctic region for bio-prospecting |
| title_fullStr | Discovery of cold-active protease from psychrophilic bacteria isolated from Antarctic region for bio-prospecting |
| title_full_unstemmed | Discovery of cold-active protease from psychrophilic bacteria isolated from Antarctic region for bio-prospecting |
| title_short | Discovery of cold-active protease from psychrophilic bacteria isolated from Antarctic region for bio-prospecting |
| title_sort | discovery of cold-active protease from psychrophilic bacteria isolated from antarctic region for bio-prospecting |
| url | http://journalarticle.ukm.my/15699/ http://journalarticle.ukm.my/15699/ http://journalarticle.ukm.my/15699/1/49_01_06.pdf |