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International Journal of Biological Macromolecules
Volume 164, 2020, Pages 3446-3453

Fibrinolytic enzyme from Arthrospira platensis cultivated in medium culture supplemented with corn steep liquor

Priscila Danielly Santos deBarrosa, Pablo Eugênio Costa eSilvab, Thiago PajeúNascimentoa, Romero Marcos Pedrosa BrandãoCostac, Raquel PedrosaBezerraa, Ana Lúcia FigueiredoPortoa,b

Department of Morphology and Animal Physiology, Federal Rural University of Pernambuco-UFRPE, Dom Manoel de Medeiros Ave., Recife, PE 52171-900, Brazil.

Abstract

Artrhospira (Spirulinaplatensis produced fibrinolytic enzyme under mixotrophic conditions using corn steep liquor (CSL). The enzyme was extracted, purified by combination of two chromatographic techniques and biochemically characterized. Maximum fibrinolytic production (268.14 U mg-1) was obtained using liquid medium culture composed by 0.2% CLS after 10th day of cultivation. Fibrinolytic activity was higher when extracted by homogenization methods and was purified 32.72–fold with specific activity of 7988 U mg-1. Fibrin zymography showed an active band, indicated acts as a plasmin-like protein with molecular weight of 72 kDa. Fibrinolytic enzyme have optimum pH of 6.0, stable in the range of 6.0 to 10.0 during 24 h and optimum temperature at 40 °C with a stability below 50°C. Fibrinolytic enzyme is a serine metalloprotease by to be enhanced by Fe2+ and inhibited by PMSF. The enzyme has higher enzymatic activity than most other fibrinolytic enzymes and is stable at temperature and pH human physiological. Overall, the fibrinolytic enzyme from Aplatensis has attractive biochemical properties to potential applications in the treatment of thrombosis.

Keywords: Photosynthetic microorganisms, Cyanobacterium, Serine metalloprotease, Thrombosis, Purification.

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