Static Magnetic Field Effects on Proteases With Fibrinolytic Activity Produced by Mucor Subtilissimus

被引:5
作者
Albuquerque, Wendell [1 ]
Nascimento, Thiago [2 ]
Brandao-Costa, Romero [1 ]
Fernandes, Thiago [3 ]
Porto, Ana [1 ]
机构
[1] Univ Fed Rural Pernambuco, Dept Anim Morphol & Physiol, Recife, PE, Brazil
[2] Univ Fed Rural Pernambuco, LIKA, Recife, PE, Brazil
[3] Univ Fed Rural Pernambuco, Dept Biophys & Radiobiol, Av Prof Luiz Freire,1000 Cidade Univ, Recife, PE, Brazil
关键词
magnetic; protein; degradation; fibrinolysis; fibrin; RADICAL RECOMBINATION REACTIONS; ETHANOLAMINE AMMONIA-LYASE; FERMENTATION; POLYMERIZATION; PURIFICATION; SPORULATION; MECHANISM; CELLULASE; EXPOSURE; ENZYMES;
D O I
10.1002/bem.22016
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
The influence of a static magnetic field (SMF) on crude enzyme extracts with proteolytic activity is described and discussed. Proteolytic enzymes, which hydrolyze peptide bonds, and fibrinolytic enzymes, which dissolve fibrin clots, have industrial relevance, and applicability dependent on improvements of productivity and activity. We investigated whether a moderate SMF affects proteolysis in different in vitro tests: general proteolysis of azocasein substrate, and static and dynamic fibrinolytic processes (to compare fibrin gel configuration under exposure). Crude enzyme extracts, obtained from solid state fermentation of Mucor subtilissimus UCP (Universidade Catolica de Pernambuco, Recife, Brazil) 1262, were used to carry out assays under slightly heterogeneous fields: a varied vertical SMF (for tests in Eppendorf tubes, from 0.100 to 0.170 T) and a varied horizontal SMF (for tests in Petri dishes, from 0.01 to 0.122 T), generated by two permanent magnets (NdFeB alloy). Results showed significant differences (P< 0.05) in static fibrinolysis assays after 24 h of exposure. The mean diameter of halos of fibrin degradation in the treated group increased by 21% compared to the control group; and the pixel number count of fibrin consumption (in a computational analysis of the area of each halo) enhanced by 30% with exposure. However, in dynamic fibrinolysis assays, no effects of SMF were observed. These results suggest a response of fibrin monomers to the SMF as a possible cause of the observed effects. (C) 2016 Wiley Periodicals, Inc.
引用
收藏
页码:109 / 120
页数:12
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