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Author Mahajan, Prafulla M. ♦ Nayak, Shubhada ♦ Lele, Smita S.
Source World Health Organization (WHO)-Global Index Medicus
Content type Text
Publisher Elsevier
File Format HTM / HTML
Language English
Difficulty Level Medium
Subject Domain (in DDC) Computer science, information & general works ♦ Library & information sciences ♦ Natural sciences & mathematics ♦ Chemistry & allied sciences ♦ Life sciences; biology ♦ Physiology & related subjects ♦ Biochemistry ♦ Natural history of organisms ♦ Microorganisms, fungi & algae ♦ Technology ♦ Medicine & health ♦ Human physiology ♦ Pharmacology and therapeutics ♦ Diseases ♦ Chemical engineering ♦ Manufacture for specific uses ♦ Precision instruments & other devices
Subject Domain (in MeSH) Bacteria ♦ Organisms ♦ Amino Acids, Peptides, and Proteins ♦ Nucleic Acids, Nucleotides, and Nucleosides ♦ Chemical Actions and Uses ♦ Chemicals and Drugs ♦ Investigative Techniques ♦ Analytical, Diagnostic and Therapeutic Techniques and Equipment ♦ Physical Phenomena ♦ Chemical Phenomena ♦ Biological Sciences ♦ Information Science ♦ Information Science
Subject Keyword Discipline Biomedical Engineering ♦ Discipline Microbiology ♦ Bacillus Subtilis ♦ Enzymology ♦ Genetics ♦ Isolation & Purification ♦ Base Sequence ♦ Enzyme Activation ♦ Drug Effects ♦ Enzyme Inhibitors ♦ Pharmacology ♦ Enzyme Stability ♦ Fibrin ♦ Metabolism ♦ Fibrinolytic Agents ♦ Hydrogen-ion Concentration ♦ Molecular Sequence Data ♦ Molecular Weight ♦ Rna, Ribosomal, 16s ♦ Temperature ♦ Journal Article ♦ Research Support, Non-u.s. Gov't
Abstract Fibrinolytic enzymes are important in treatment of cardiovascular diseases. The present work reports isolation, screening and identification of marine cultures for production of fibrinolytic enzymes. A potent fibrinolytic enzyme-producing bacterium was isolated from marine niches and identified as Bacillus subtilis ICTF-1 on the basis of the 16S rRNA gene sequencing and biochemical properties. Further, media optimization using L(18)-orthogonal array method resulted in enhanced production of fibrinolytic enzyme (8814 U/mL) which was 2.6 fold higher than in unoptimized medium (3420 U/mL). In vitro assays revealed that the enzyme could catalyze blood clot lysis effectively, indicating that this enzyme could be a useful thrombolytic agent. A fibrinolytic enzyme was purified from the culture supernatant to homogeneity by three step procedures with a 34.42-fold increase in specific activity and 7.5% recovery. This purified fibrinolytic enzyme had molecular mass of 28 kDa, optimal temperature and pH at 50 °C and 9, respectively. It was stable at pH 5.0-11.0 and temperature of 25-37 °C. The enzyme activity was activated by Ca(2+) and obviously inhibited by Zn(2+), Fe(3)(+), Hg(2+) and PMSF. The purified fibrinolytic enzyme showed high stability towards various surfactants and was relatively stable towards oxidizing agent. Considering these properties purified fibrinolytic enzyme also finds potential application in laundry detergents in addition to thrombolytic agent. The gene encoding fibrinolytic enzyme was isolated and its DNA sequence was determined. Compared the full DNA sequence with those in NCBI, it was considered to be a subtilisin like serine-protease.
Description Country affiliation: India
Author Affiliation: Mahajan PM ( Food Engineering and Technology Department, Institute of Chemical Technology, NP Marg, Matunga, Mumbai-400 019, India.)
ISSN 13891723
Educational Role Student ♦ Teacher
Age Range above 22 year
Educational Use Reading ♦ Research ♦ Self Learning
Interactivity Type Expositive
Education Level UG and PG
Learning Resource Type Article
Publisher Date 2012-03-01
Publisher Place Japan
e-ISSN 13474421
Journal Journal of Bioscience and Bioengineering
Volume Number 113
Issue Number 3

Source: WHO-Global Index Medicus