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Effective Photoinactivation of Alpha‐Amylase, Catalase and Urease at 222 nm Emitted by an KrCl‐Excimer Lamp
Author(s) -
Clauß Marcus,
Grotjohann Norbert
Publication year - 2008
Publication title -
clean – soil, air, water
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.444
H-Index - 66
eISSN - 1863-0669
pISSN - 1863-0650
DOI - 10.1002/clen.200700184
Subject(s) - irradiation , chemistry , excimer , catalase , mercury vapor lamp , fluence , urease , photochemistry , enzyme , materials science , fluorescence , ion , optics , biochemistry , optoelectronics , organic chemistry , physics , nuclear physics
Abstract The inactivation of enzymes is of great interest for many industrial applications. The effectiveness of photoinactivation of alpha‐amylase, catalase, and urease with 222 nm radiation was investigated in comparison to that at 254 nm. The enzymes were irradiated with different fluence rates of 222 nm radiation emitted by a KrCl‐excimer lamp and with 254 nm radiation produced by a low‐pressure mercury lamp. The relative activities were calculated before and after irradiation. Degradation caused by UV‐radiation was assessed by SDS‐PAGE analysis. The results clearly demonstrated that inactivation of the proteins is much more effective with the 222 nm excimer lamp compared to the 254 nm mercury lamp. Irradiation with the excimer lamp and a UV‐fluence rate of 1000 J/m 2 was sufficient to reduce the relative activities of amylase and urease to 15% and that of catalase to 60%. After irradiation with 4000 J/m 2 , the enzyme activity was almost completely inhibited. In contrast, after irradiation with the mercury lamp with an UV‐fluence rate of 4000 J/m 2 , the relative activity was still above 85%. The gel patterns showed no visible degradation after irradiation at 254 nm, but a strong and unspecific degradation was obvious after treatment at 222 nm, presumably caused by cleavage of the peptide bonds.