Literature DB >> 32882274

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

Priscila Danielly Santos de Barros1, Pablo Eugênio Costa E Silva2, Thiago Pajeú Nascimento1, Romero Marcos Pedrosa Brandão Costa3, Raquel Pedrosa Bezerra4, Ana Lúcia Figueiredo Porto5.   

Abstract

Artrhospira (Spirulina) platensis 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 A. platensis has attractive biochemical properties to potential applications in the treatment of thrombosis.
Copyright © 2020 Elsevier B.V. All rights reserved.

Entities:  

Keywords:  Cyanobacterium; Photosynthetic microorganisms; Purification; Serine metalloprotease; Thrombosis

Mesh:

Substances:

Year:  2020        PMID: 32882274     DOI: 10.1016/j.ijbiomac.2020.08.217

Source DB:  PubMed          Journal:  Int J Biol Macromol        ISSN: 0141-8130            Impact factor:   6.953


  6 in total

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Review 6.  Marine Microbial Fibrinolytic Enzymes: An Overview of Source, Production, Biochemical Properties and Thrombolytic Activity.

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