Isolation of alkaliphilic microbes producing highly alkaline thermostable protease

For many decades, alkaliphilic bacteria that can produce highly alkaline thermostable protease had been the focus of the intense research since they were able to perform well under high temperature and pH during many industrial processes. Proteolytic bacteria that were isolated from Selayang and Kua...

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Main Author: Choo, Kin Yan
Format: Project Paper Report
Language:English
Published: 2015
Online Access:http://psasir.upm.edu.my/id/eprint/85111/
http://psasir.upm.edu.my/id/eprint/85111/1/FBSB%202015%20100%20-%20IR.pdf
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author Choo, Kin Yan
author_facet Choo, Kin Yan
author_sort Choo, Kin Yan
building UPM Institutional Repository
collection Online Access
description For many decades, alkaliphilic bacteria that can produce highly alkaline thermostable protease had been the focus of the intense research since they were able to perform well under high temperature and pH during many industrial processes. Proteolytic bacteria that were isolated from Selayang and Kuala Kubu Bharu hot springs in Malaysia were screened using skim milk agar plates. Isolates which showed better proteolytic activity were chosen for further identification. Bacillus licheniformis strain 1 and Bacillus licheniformis strain H were identified by using gram staining, biochemical tests and 16S rDNA sequence analysis. Protease produced by Bacillus licheniformis strain 1 reached optimum proteolytic activity at 65°C, pH 9. Its stability showed broad temperature ranges between 40 to 65°C, whereas it was stable from pH 4 to 6 for pH ranges. On the other hand, the maximum proteolytic activity showed by Bacillus licheniformis strain H was at 65°C, pH 9. Protease produced by this strain also had the potential to be stable over wide ranges of temperature and pH, that were between 40 to 60°C and from pH 4 to 11.
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spelling upm-851112021-12-27T04:17:43Z http://psasir.upm.edu.my/id/eprint/85111/ Isolation of alkaliphilic microbes producing highly alkaline thermostable protease Choo, Kin Yan For many decades, alkaliphilic bacteria that can produce highly alkaline thermostable protease had been the focus of the intense research since they were able to perform well under high temperature and pH during many industrial processes. Proteolytic bacteria that were isolated from Selayang and Kuala Kubu Bharu hot springs in Malaysia were screened using skim milk agar plates. Isolates which showed better proteolytic activity were chosen for further identification. Bacillus licheniformis strain 1 and Bacillus licheniformis strain H were identified by using gram staining, biochemical tests and 16S rDNA sequence analysis. Protease produced by Bacillus licheniformis strain 1 reached optimum proteolytic activity at 65°C, pH 9. Its stability showed broad temperature ranges between 40 to 65°C, whereas it was stable from pH 4 to 6 for pH ranges. On the other hand, the maximum proteolytic activity showed by Bacillus licheniformis strain H was at 65°C, pH 9. Protease produced by this strain also had the potential to be stable over wide ranges of temperature and pH, that were between 40 to 60°C and from pH 4 to 11. 2015 Project Paper Report NonPeerReviewed text en http://psasir.upm.edu.my/id/eprint/85111/1/FBSB%202015%20100%20-%20IR.pdf Choo, Kin Yan (2015) Isolation of alkaliphilic microbes producing highly alkaline thermostable protease. [Project Paper Report]
spellingShingle Choo, Kin Yan
Isolation of alkaliphilic microbes producing highly alkaline thermostable protease
title Isolation of alkaliphilic microbes producing highly alkaline thermostable protease
title_full Isolation of alkaliphilic microbes producing highly alkaline thermostable protease
title_fullStr Isolation of alkaliphilic microbes producing highly alkaline thermostable protease
title_full_unstemmed Isolation of alkaliphilic microbes producing highly alkaline thermostable protease
title_short Isolation of alkaliphilic microbes producing highly alkaline thermostable protease
title_sort isolation of alkaliphilic microbes producing highly alkaline thermostable protease
url http://psasir.upm.edu.my/id/eprint/85111/
http://psasir.upm.edu.my/id/eprint/85111/1/FBSB%202015%20100%20-%20IR.pdf