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Production and characterization of protease from halophilic virgibacillus species CD6

In enzyme production industries, the major challenges that hinder the efficient and economic commercial scale application of proteases are their stability in broad range of pH, temperature, salinity, as well as their optimal activity in the presence of metal ions, organic solvents and detergents. Mo...

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Main Author: Lam, Ming Quan
Format: Thesis
Language:English
Published: 2017
Subjects:
TP Chemical technology
Online Access:http://eprints.utm.my/id/eprint/78664/1/LamMingQuanMFBME2017.pdf
http://eprints.utm.my/id/eprint/78664/
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spelling my.utm.786642018-08-29T07:35:44Z http://eprints.utm.my/id/eprint/78664/ Production and characterization of protease from halophilic virgibacillus species CD6 Lam, Ming Quan TP Chemical technology In enzyme production industries, the major challenges that hinder the efficient and economic commercial scale application of proteases are their stability in broad range of pH, temperature, salinity, as well as their optimal activity in the presence of metal ions, organic solvents and detergents. Moreover, the enzyme purification steps also contribute to the cost of production. To overcome this problem, characterization and production of crude protease with attractive properties from wild bacterial isolate could be an alternative as it is a more cost-effective way compared to production of protease that involves purification steps and protein engineering approach. Therefore, crude protease of Virgibacillus sp. CD6 isolated from salted-fish was characterized in this study using azocasein assay and bioinformatics tools. Protease production was found to be highest when using soybean meal and yeast extract as nitrogen source compared to other organic nitrogen sources. The protease exhibited vast range of stability with optimum activity at 10.0 % (w/v) NaCl, 60ºC, pH 7 and 10, indicating its polyextremophilicity. The enzyme activity was enhanced by Mg2+, Mn2+, Cd2+ and Al3+. Both PMSF and EDTA hindered protease activity, denoting the presence of serine protease and metalloprotease properties respectively. High protease stability (>80%) was demonstrated in presence of organic solvents and detergent constituents investigated, and surprisingly it is exceptionally compatible with commercial detergents. Phylogenetic analyses revealed that proteases of Virgibacillus sp. demonstrated far distance relationship with other species, which worth for further exploration. Attributes of this protease can actualize necessity of searching superlative enzymes from extremophiles for diverse applications, particularly in detergent industry. 2017-01 Thesis NonPeerReviewed application/pdf en http://eprints.utm.my/id/eprint/78664/1/LamMingQuanMFBME2017.pdf Lam, Ming Quan (2017) Production and characterization of protease from halophilic virgibacillus species CD6. Masters thesis, Universiti Teknologi Malaysia, Faculty of Biosciences and Medical Engineering. http://dms.library.utm.my:8080/vital/access/manager/Repository/vital:109608
institution Universiti Teknologi Malaysia
building UTM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Teknologi Malaysia
content_source UTM Institutional Repository
url_provider http://eprints.utm.my/
language English
topic TP Chemical technology
spellingShingle TP Chemical technology
Lam, Ming Quan
Production and characterization of protease from halophilic virgibacillus species CD6
description In enzyme production industries, the major challenges that hinder the efficient and economic commercial scale application of proteases are their stability in broad range of pH, temperature, salinity, as well as their optimal activity in the presence of metal ions, organic solvents and detergents. Moreover, the enzyme purification steps also contribute to the cost of production. To overcome this problem, characterization and production of crude protease with attractive properties from wild bacterial isolate could be an alternative as it is a more cost-effective way compared to production of protease that involves purification steps and protein engineering approach. Therefore, crude protease of Virgibacillus sp. CD6 isolated from salted-fish was characterized in this study using azocasein assay and bioinformatics tools. Protease production was found to be highest when using soybean meal and yeast extract as nitrogen source compared to other organic nitrogen sources. The protease exhibited vast range of stability with optimum activity at 10.0 % (w/v) NaCl, 60ºC, pH 7 and 10, indicating its polyextremophilicity. The enzyme activity was enhanced by Mg2+, Mn2+, Cd2+ and Al3+. Both PMSF and EDTA hindered protease activity, denoting the presence of serine protease and metalloprotease properties respectively. High protease stability (>80%) was demonstrated in presence of organic solvents and detergent constituents investigated, and surprisingly it is exceptionally compatible with commercial detergents. Phylogenetic analyses revealed that proteases of Virgibacillus sp. demonstrated far distance relationship with other species, which worth for further exploration. Attributes of this protease can actualize necessity of searching superlative enzymes from extremophiles for diverse applications, particularly in detergent industry.
format Thesis
author Lam, Ming Quan
author_facet Lam, Ming Quan
author_sort Lam, Ming Quan
title Production and characterization of protease from halophilic virgibacillus species CD6
title_short Production and characterization of protease from halophilic virgibacillus species CD6
title_full Production and characterization of protease from halophilic virgibacillus species CD6
title_fullStr Production and characterization of protease from halophilic virgibacillus species CD6
title_full_unstemmed Production and characterization of protease from halophilic virgibacillus species CD6
title_sort production and characterization of protease from halophilic virgibacillus species cd6
publishDate 2017
url http://eprints.utm.my/id/eprint/78664/1/LamMingQuanMFBME2017.pdf
http://eprints.utm.my/id/eprint/78664/
http://dms.library.utm.my:8080/vital/access/manager/Repository/vital:109608
_version_ 1643657967619276800
score 13.211869

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