Static magnetic field effects on proteases with fibrinolytic activity produced by Mucor subtilissimus

Abstract

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 Católica 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. Bioelectromagnetics. 38:109-120, 2017. © 2016 Wiley Periodicals, Inc.

Production, Kinetic/Thermodynamic Study, and Evaluation of the Influence of Static Magnetic Field on Kinetic Parameters of β-Fructofuranosidase from Aspergillus tamarii Kita UCP 1279 Produced by Solid-State Fermentation

“…Similar qualitative behavior for K m was observed by Liu et al [ 14 ] when the immobilized α-amylase kinetic parameters in the presence of 0.15 T were evaluated. However, other authors, such as Albuquerque et al [ 17 ], did not observe significant differences in K m and V max for fibrinolytic protease from Mucor subtilissimus and a negative impact of SMF was evidenced by increase in K m and decrease in V max , as reported by Sun et al [ 31 ] for a vegetable pectinase. Among the different mechanisms involved in modifications of biocatalyst activity by exposure to SMF, the radical pair recombination has been the preferred explanation, though it requires conditions at moderate magnetic fields to be effective [ 17 , 32 ], which is the case of the present experiment.…”

“…Some authors observed a positive impact of exposure to the enzyme on magnetic fields on enzyme kinetics [ 14 , 15 ], evidenced by an increase of affinity to correspondent substrate, which can favor several bioprocesses. The chemical or physical modifications in the enzymatic structural modification after magnetic flux have been studied in different industrial interest enzymes, such as lipases [ 16 ] and amylases [ 14 ], and clinical interest enzymes, such as fibrinolytic proteases [ 17 ]. However, to best of our knowledge, no studies exist evaluating this influence on FOS forming enzymes.…”

Production of fibrinogenolytic and fibrinolytic enzymes by a strain of <i>Penicillium</i> sp. isolated from contaminated soil with industrial effluent

“…Health Sciences, v. 41, e40606, 2019 The literature describes enzymes isolated from fungi that have fibrinolytic activity. Albuquerque, Nascimento, Brandão-Costa, Fernandes, and Porto (2017), reported that the crude extract of Mucor subtilissimus showed fibrinolytic activity presenting degradation halos in fibrin dishes. A new fibrinolytic protease, AfeE, with strong thrombolytic activity, was purified from Streptomyces sp.…”