Enhanced production, purification and biochemical characterization of therapeutic potential fibrinolytic enzyme from a new Bacillus flexus from marine environment

Objectives: The main aim of this study is to isolate and characterize fibrinolytic enzyme from Bacillus flexus. Methods: Fish meal of Sardinella longiceps and anchovy was optimized using a two-level full factorial design (25) and response surface methodology. The significant physical factors and nut...

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Main Authors: Dunia A. Al Farraj, T. Sujin Jeba Kumar, Ponnuswamy Vijayaraghavan, Mohamed Soliman Elshikh, Roua M. Alkufeidy, Noorah A. Alkubaisi, Maryam K. Alshammari
Format: Article
Language:English
Published: Elsevier 2020-10-01
Series:Journal of King Saud University: Science
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S1018364720302718
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author Dunia A. Al Farraj
T. Sujin Jeba Kumar
Ponnuswamy Vijayaraghavan
Mohamed Soliman Elshikh
Roua M. Alkufeidy
Noorah A. Alkubaisi
Maryam K. Alshammari
author_facet Dunia A. Al Farraj
T. Sujin Jeba Kumar
Ponnuswamy Vijayaraghavan
Mohamed Soliman Elshikh
Roua M. Alkufeidy
Noorah A. Alkubaisi
Maryam K. Alshammari
author_sort Dunia A. Al Farraj
collection DOAJ
description Objectives: The main aim of this study is to isolate and characterize fibrinolytic enzyme from Bacillus flexus. Methods: Fish meal of Sardinella longiceps and anchovy was optimized using a two-level full factorial design (25) and response surface methodology. The significant physical factors and nutrient sources (peptone, maltose, and magnesium chloride) were identified by statistical approach. The properties of a purified enzyme including their effect at different temperature, pH and the effect of metal ions were evaluated. Results: Enzyme yield was improved 3.5 fold than unoptimized medium. Central composite design optimized culture medium enhanced enzyme yield (4711 ± 29.3 U/g of substrate). The fibrinolytic enzyme was highly active at alkaline pH (8.0), 50 °C and the molecular weight was 32 kDa. Conclusions: From these findings, it concludes that this fibrinolytic enzyme could be a novel potent thrombolytic agent.
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spelling doaj.art-7fdc2697993e4009b5a22b3843e6413a2022-12-22T00:48:51ZengElsevierJournal of King Saud University: Science1018-36472020-10-0132731743180Enhanced production, purification and biochemical characterization of therapeutic potential fibrinolytic enzyme from a new Bacillus flexus from marine environmentDunia A. Al Farraj0T. Sujin Jeba Kumar1Ponnuswamy Vijayaraghavan2Mohamed Soliman Elshikh3Roua M. Alkufeidy4Noorah A. Alkubaisi5Maryam K. Alshammari6Department of Botany and Microbiology, College of Sciences, King Saud University, P.O. Box 22452, Riyadh 11495, Saudi Arabia; Corresponding author.Bioprocess Engineering Division, Smykon Biotech Pvt LtD, Nagercoil, Kanyakumari, Tamil Nadu 629201, IndiaBioprocess Engineering Division, Smykon Biotech Pvt LtD, Nagercoil, Kanyakumari, Tamil Nadu 629201, IndiaDepartment of Botany and Microbiology, College of Sciences, King Saud University, P.O. Box 22452, Riyadh 11495, Saudi ArabiaDepartment of Botany and Microbiology, College of Sciences, King Saud University, P.O. Box 22452, Riyadh 11495, Saudi ArabiaDepartment of Botany and Microbiology, College of Sciences, King Saud University, P.O. Box 22452, Riyadh 11495, Saudi ArabiaDepartment of Botany and Microbiology, College of Sciences, King Saud University, P.O. Box 22452, Riyadh 11495, Saudi ArabiaObjectives: The main aim of this study is to isolate and characterize fibrinolytic enzyme from Bacillus flexus. Methods: Fish meal of Sardinella longiceps and anchovy was optimized using a two-level full factorial design (25) and response surface methodology. The significant physical factors and nutrient sources (peptone, maltose, and magnesium chloride) were identified by statistical approach. The properties of a purified enzyme including their effect at different temperature, pH and the effect of metal ions were evaluated. Results: Enzyme yield was improved 3.5 fold than unoptimized medium. Central composite design optimized culture medium enhanced enzyme yield (4711 ± 29.3 U/g of substrate). The fibrinolytic enzyme was highly active at alkaline pH (8.0), 50 °C and the molecular weight was 32 kDa. Conclusions: From these findings, it concludes that this fibrinolytic enzyme could be a novel potent thrombolytic agent.http://www.sciencedirect.com/science/article/pii/S1018364720302718Fibrinolytic enzymeBacillusCheap substratesBlood clotFibrinolytic agent
spellingShingle Dunia A. Al Farraj
T. Sujin Jeba Kumar
Ponnuswamy Vijayaraghavan
Mohamed Soliman Elshikh
Roua M. Alkufeidy
Noorah A. Alkubaisi
Maryam K. Alshammari
Enhanced production, purification and biochemical characterization of therapeutic potential fibrinolytic enzyme from a new Bacillus flexus from marine environment
Journal of King Saud University: Science
Fibrinolytic enzyme
Bacillus
Cheap substrates
Blood clot
Fibrinolytic agent
title Enhanced production, purification and biochemical characterization of therapeutic potential fibrinolytic enzyme from a new Bacillus flexus from marine environment
title_full Enhanced production, purification and biochemical characterization of therapeutic potential fibrinolytic enzyme from a new Bacillus flexus from marine environment
title_fullStr Enhanced production, purification and biochemical characterization of therapeutic potential fibrinolytic enzyme from a new Bacillus flexus from marine environment
title_full_unstemmed Enhanced production, purification and biochemical characterization of therapeutic potential fibrinolytic enzyme from a new Bacillus flexus from marine environment
title_short Enhanced production, purification and biochemical characterization of therapeutic potential fibrinolytic enzyme from a new Bacillus flexus from marine environment
title_sort enhanced production purification and biochemical characterization of therapeutic potential fibrinolytic enzyme from a new bacillus flexus from marine environment
topic Fibrinolytic enzyme
Bacillus
Cheap substrates
Blood clot
Fibrinolytic agent
url http://www.sciencedirect.com/science/article/pii/S1018364720302718
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