{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,4]],"date-time":"2026-05-04T12:08:36Z","timestamp":1777896516772,"version":"3.51.4"},"reference-count":32,"publisher":"Hindawi Limited","license":[{"start":{"date-parts":[[2013,1,1]],"date-time":"2013-01-01T00:00:00Z","timestamp":1356998400000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/3.0\/"}],"funder":[{"name":"Department of Science and Technology (DST)","award":["21206133"],"award-info":[{"award-number":["21206133"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["BioMed Research International"],"published-print":{"date-parts":[[2013]]},"abstract":"<jats:p><jats:italic>Stenotrophomonas maltophilia<\/jats:italic>PM102 (NCBI GenBank Acc. no. JQ797560) is capable of growth on trichloroethylene as the sole carbon source. In this paper, we report the purification and characterisation of oxygenase present in the PM102 isolate. Enzyme activity was found to be induced 10.3-fold in presence of 0.7\u2009mM copper with a further increment to 14.96-fold in presence of 0.05\u2009mM NADH. Optimum temperature for oxygenase activity was recorded at<mml:math xmlns:mml=\"http:\/\/www.w3.org\/1998\/Math\/MathML\" id=\"M1\"><mml:msup><mml:mn>36<\/mml:mn><mml:mo>\u2218<\/mml:mo><\/mml:msup><mml:mtext>C<\/mml:mtext><\/mml:math>. The reported enzyme was found to have enhanced activity at pH 5 and pH 8, indicating presence of two isoforms. Maximum activity was seen on incubation with benzene compared to other substrates like TCE, chloroform, toluene, hexane, and petroleum benzene.<mml:math xmlns:mml=\"http:\/\/www.w3.org\/1998\/Math\/MathML\" id=\"M2\"><mml:mrow><mml:msub><mml:mrow><mml:mi>K<\/mml:mi><\/mml:mrow><mml:mrow><mml:mi>m<\/mml:mi><\/mml:mrow><\/mml:msub><\/mml:mrow><\/mml:math>and<mml:math xmlns:mml=\"http:\/\/www.w3.org\/1998\/Math\/MathML\" id=\"M3\"><mml:mrow><mml:msub><mml:mrow><mml:mi>V<\/mml:mi><\/mml:mrow><mml:mrow><mml:mtext>max<\/mml:mtext><\/mml:mrow><\/mml:msub><\/mml:mrow><\/mml:math>for benzene were 3.8\u2009mM and 340\u2009U\/mg\/min and those for TCE were 2.1\u2009mM and 170\u2009U\/mg\/min. The crude enzyme was partially purified by ammonium sulphate precipitation followed by dialysis. Zymogram analysis revealed two isoforms in the 70% purified enzyme fraction. The activity stain was more prominent when the native gel was incubated in benzene as substrate in comparison to TCE. Crude enzyme and purified enzyme fractions were assayed for TCE degradation by the Fujiwara test. TCE biotransformation products were analysed by FT-IR spectroscopy.<\/jats:p>","DOI":"10.1155\/2013\/723680","type":"journal-article","created":{"date-parts":[[2013,9,8]],"date-time":"2013-09-08T21:01:35Z","timestamp":1378674095000},"page":"1-9","source":"Crossref","is-referenced-by-count":10,"title":["Copper Enhanced Monooxygenase Activity and FT-IR Spectroscopic Characterisation of Biotransformation Products in Trichloroethylene Degrading Bacterium:<i>Stenotrophomonas maltophilia<\/i>PM102"],"prefix":"10.1155","volume":"2013","author":[{"given":"Piyali","family":"Mukherjee","sequence":"first","affiliation":[{"name":"Department of Biotechnology, Burdwan University, Golapbag, Burdwan, West Bengal, 713104, India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Pranab","family":"Roy","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, Haldia Institute of Technology, Haldia, West Bengal, 721657, 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