Isolation and Identification Fibrinolytic Protease Endophytic Fungi from Hibiscus Leaves in Shah Alam
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Isolation and Identification Fibrinolytic Protease Endophytic Fungi from Hibiscus Leaves in Shah Alam

Authors: Mohd Sidek Ahmad, Zainon Mohd Noor, Zaidah Zainal Ariffin

Abstract:

Fibrin degradation is an important part in prevention or treatment of intravascular thrombosis and cardiovascular diseases. Plasmin like fibrinolytic enzymes has given new hope to patient with cardiovascular diseases by treating fibrin aggregation related diseases with traditional plasminogen activator which have many side effects. Various researches involving wide range of sources for production of fibrinolytic proteases, from bacteria, fungi, insects and fermented foods. But few have looked into endophytic fungi as a potential source. Sixteen (16) endophytic fungi were isolated from Hibiscus sp. leaves from six different locations in Shah Alam, Selangor. Only two endophytic fungi, FH3 and S13 showed positive fibrinolytic protease activities. FH3 produced 5.78cm and S13 produced 4.48cm on Skim Milk Agar after 4 days of incubation at 27°C. Fibrinolytic activity was observed; 3.87cm and 1.82cm diameter clear zone on fibrin plate of FH3 and S13 respectively. 18srRNA was done for identification of the isolated fungi with positive fibrinolytic protease. S13 had the highest similarity (100%) to that of Penicillium citrinum strain TG2 and FH3 had the highest similarity (99%) to that of Fusarium sp. FW2PhC1, Fusarium sp. 13002, Fusarium sp. 08006, Fusarium equiseti strain Salicorn 8 and Fungal sp. FCASAn-2. Media composition variation showed the effects of carbon nitrogen on protein concentration, where the decrement of 50% of media composition caused drastic decrease in protease of FH3 from 1.081 to 0.056 and also S13 from 2.946 to 0.198.

Keywords: Isolation, identification, fibrinolytic protease, endophytic fungi, Hibiscus leaves.

Digital Object Identifier (DOI): doi.org/10.5281/zenodo.1096175

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References:


[1] Bin W., Licheng W., Daijie C., Zhijun Y., Minyu L., Purification and characterization of a novel fibrinolytic protease from Fusarium sp. CPCC 480097. J Ind Microbiol Biotechnol, 2009, 36:451–459.
[2] Fengxia L., Zhaoxin L., Xiaomei B., Zhengying Y., Yufeng W., Yaping L., Yao G., Purification and characterization of a novel anticoagulant and fibrinolytic enzyme produced by endophytic bacterium Paenibacillus polymyxa EJS-3. Thrombosis Research, 126, 2010, e349– e355.
[3] Tzu-Wen L., Jia-Lin H., San-Lang W., Production and purification of a protease, a chitosanase, and chitin oligosaccharides by Bacillus cereus TKU022 fermentation. Carbohydrate Research, 362, 2012, 38–46.
[4] Balachandran C., Duraipandiyan V., Ignacimuthu S., Purification and characterization of protease enzyme from actinomycetes and its cytotoxic effect on cancer cell line (A549). Asian Pacific Journal of Tropical Biomedicine, 2012, S392-S400.
[5] Kumaran S., Palani P., Chellaram C., Prem Anand T., Kaviyarasan V., Screening of fibrinolytic protease from south indian isolates of Ganoderma lucidum. International Journal of Pharma and Bio Sciences Vol 2 Issue 1 Jan-Mar, 2011, ISSN 0975-6299.
[6] Devchand N. A., Virendra K. R. Ultrasound stimulated production of a fibrinolytic enzyme Ultrasonics Sonochemistry, 21 2014, 182–188.
[7] Astrup, T.; Mullertz, S. The fibrin plate method for estimating fibrinolytic activity. Arch. Biochem. Biophys., 1952, 40, 346–351.
[8] Sugimoto, S.; Fujii, T.; Morimiya, T.; Johdo, O.; Nakamura, T. The fibrinolytic activity of a novel protease derived from a tempeh producing fungus, Fusarium sp. BLB. Biosci. Biotechnol. Biochem., 2007, 71, 2184-2189.
[9] Shirasaka, N.; Naitou, M.; Okamura, K.; Kusuda, M.; Fukuta, Y.; Terashita, T. Purification and characterization of a fibrinolytic protease from Aspergillus oryzae KSK-3. Springer Mycoscience, 2012, 1, 16-17.
[10] Bhargavi P. L., Prakasham R. S. A fibrinolytic, alkaline and thermostable metalloprotease from the newly isolated Serratia sp RSPB11. International Journal of Biological Macromolecules, 2013, 1- 33.
[11] Pekkarinen A., Mannonen L., Jones B. L., Niku-Paavola M.-L. Production of Proteases by Fusarium Species Grown on Barley Grains and in Media Containing Cereal Proteins Journal of Cereal Science, 31, 2000, 253–261.