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The work presented here describes the ability of A. acidocaldarius to reduce the concentration of the phenolic compounds: phenol, ferulic acid, \u03c1-coumaric acid and sinapinic acid during growth conditions. The extent and rate of the removal of these compounds were significantly increased by the presence of micro-molar copper concentrations, suggesting activity by copper oxidases that have been identified in the genome of A. acidocaldarius. Substrate removal kinetics was first order for phenol, ferulic acid, \u03c1-coumaric acid and sinapinic acid in the presence of 50\u00a0\u03bcM copper sulfate. In addition, laccase enzyme assays of cellular protein fractions suggested significant activity on a lignin analog between the temperatures of 45 and 90\u00a0\u00b0C. This work shows the potential for A. acidocaldarius to degrade phenolic compounds, demonstrating potential relevance to biofuel production and other industrial processes.<\/jats:p>","DOI":"10.1007\/s10295-015-1700-z","type":"journal-article","created":{"date-parts":[[2015,11,5]],"date-time":"2015-11-05T07:17:40Z","timestamp":1446707860000},"page":"13-23","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":23,"title":["Degradation of phenolic compounds by the lignocellulose deconstructing thermoacidophilic bacterium <i>Alicyclobacillus Acidocaldarius<\/i>"],"prefix":"10.1093","volume":"43","author":[{"given":"John E","family":"Aston","sequence":"first","affiliation":[{"name":"grid.417824.c 0000000100207392 Biological and Chemical Processing Department Idaho National Laboratory Idaho Falls ID USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"William A","family":"Apel","sequence":"additional","affiliation":[{"name":"grid.417824.c 0000000100207392 Biological and Chemical Processing Department Idaho National Laboratory Idaho Falls ID USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brady D","family":"Lee","sequence":"additional","affiliation":[{"name":"grid.451303.0 0000000122183491 Energy and Environment Directorate Pacific Northwest National Laboratory Richland WA USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David N","family":"Thompson","sequence":"additional","affiliation":[{"name":"grid.417824.c 0000000100207392 Biological and Chemical Processing Department Idaho National Laboratory Idaho Falls ID USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeffrey A","family":"Lacey","sequence":"additional","affiliation":[{"name":"grid.417824.c 0000000100207392 Biological and Chemical Processing Department Idaho National Laboratory Idaho Falls ID USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Deborah T","family":"Newby","sequence":"additional","affiliation":[{"name":"grid.417824.c 0000000100207392 Biological and Chemical Processing Department Idaho National Laboratory Idaho Falls ID USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David W","family":"Reed","sequence":"additional","affiliation":[{"name":"grid.417824.c 0000000100207392 Biological and Chemical Processing Department Idaho National Laboratory Idaho Falls ID USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vicki S","family":"Thompson","sequence":"additional","affiliation":[{"name":"grid.417824.c 0000000100207392 Biological and Chemical Processing Department Idaho National Laboratory Idaho Falls ID USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2016,1,1]]},"reference":[{"key":"2021033104402949000_CR1","doi-asserted-by":"publisher","first-page":"1707","DOI":"10.1099\/00221287-146-7-1707","article-title":"Arrangement and regulation of the genes for meta-pathway enzymes required for degradation of phenol in Comamonas testosteroni TA441","volume":"146","author":"Arai","year":"2000","journal-title":"Microbiology"},{"key":"2021033104402949000_CR2","doi-asserted-by":"publisher","first-page":"187","DOI":"10.1007\/s10295-009-0662-4","article-title":"A new xylanase from thermoacidophilic Alicyclobacillus sp. 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