Abstract
The hydroquinone peroxidase of the lignin decolorizing bacterium, Azotobacter beijerinckii HM121 degraded 1 g/ l of polyacrylamide ( M r 2,000,000) to small molecules ( M r less than one thousand) in 30 min in the presence of 5 mM hydrogen peroxide and 5 μM tetramethylhydroquinone. The two reaction products were purified, and identified as 1-dodecene-2, 4, 6, 8, 10-pentacarboxyamide and 1-hexadecene-2, 4, 6, 8, 10, 12, 14-heptacarboxyamide comprising 5 and 7 acrylamide units, respectively. The enzyme also degraded 1 g/ l of polyacrylic acid ( M r 450,000) in 1 h, 1 g/ l of polyethylene glycol ( M r 4,000,000) in 1 h, and 1 g/ l of polyvinyl alcohol ( M r 88,000) for 20 h. The degradation rate decreased with a decrease in the degree of polymerization of the polyethylene glycol from M r 20,000 to 400. In addition 1 g/ l of polyethylene glycol ( M r 4,000,000) was degraded in the absence of tetramethylhydroquinone, although it took 20 h.
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