Proteins are carriers of biological functions and the effects of atmospheric-pressure
non-thermal plasmas on proteins are important to applications such as sterilization
and plasma-induced apoptosis of cancer cells. Herein, we report our detailed
investigation of the effects of helium-oxygen non-thermal dielectric barrier
discharge (DBD) plasmas on the inactivation of lactate dehydrogenase (LDH) enzyme
solutions. Circular dichroism (CD) and dynamic light scattering (DLS) indicate that
the loss of activity stems from plasma-induced modification of the secondary
molecular structure as well as polymerization of the peptide chains. Raising the
treatment intensity leads to a reduced alpha-helix content, increase in the
percentage of the beta-sheet regions and random sequence, as well as gradually
decreasing LDH activity. However, the structure of the LDH plasma-treated for 300
seconds exhibits a recovery trend after storage for 24 h and its
activity also increases slightly. By comparing direct and indirect plasma
treatments, plasma-induced LDH inactivation can be attributed to reactive species
(RS) in the plasma, especially ones with a long lifetime including hydrogen
peroxide, ozone, and nitrate ion which play the major role in the alteration of the
macromolecular structure and molecular diameter in lieu of heat, UV radiation, and
charged particles.