{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T20:45:57Z","timestamp":1791146757115,"version":"4.1.0"},"reference-count":25,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2009,5,5]],"date-time":"2009-05-05T00:00:00Z","timestamp":1241481600000},"content-version":"vor","delay-in-days":4,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biotechnology Journal"],"published-print":{"date-parts":[[2009,5]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The adsorption of water and substrates to dry deposited alcohol dehydrogenase from <jats:italic>Lactobacillus brevis<\/jats:italic> (LBADH) is studied in a continuous enzymatic gas\/solid reactor. This work is aiming at obtaining a deeper and more thorough understanding of the enzyme microenvironment in the gas\/solid system of acetophenone reduction with concomitant oxidation of 2\u2010propanol. Extensive water adsorption studies showed that the effect of sucrose in the enzyme preparation on the water adsorption isotherm is significant for water activities exceeding 0.5 and reaches a factor 2 with respect to bead mass at water activity of 0.9. Significant hysteresis during water desorption is identified, resulting in up to 0.6 mg<jats:sub>water<\/jats:sub>\/mg<jats:sub>protein<\/jats:sub>, for lyophilized enzyme preparation and up to 10 mg<jats:sub>water<\/jats:sub>\/mg<jats:sub>protein<\/jats:sub> for deposited enzyme preparation. The adsorption of the substrates is quantified here for the first time. Whereas the adsorption of the main substrate, acetophenone, may reach a significant level of up to 6 mg\/mg<jats:sub>protein<\/jats:sub>, at an acetophenone activity of 0.32, the secondary substrate, 2\u2010propanol is not adsorbed at a detectable degree. The presence of water leads to a decrease of the adsorbed amount of acetophenone, by approximately 25%, at a water activity of 0.54.<\/jats:p>","DOI":"10.1002\/biot.200800291","type":"journal-article","created":{"date-parts":[[2009,5,5]],"date-time":"2009-05-05T08:13:37Z","timestamp":1241511217000},"page":"712-721","source":"Crossref","is-referenced-by-count":6,"title":["Substrate and water adsorption phenomena in a gas\/solid enzymatic reactor"],"prefix":"10.1002","volume":"4","author":[{"given":"Kerasina","family":"Dimoula","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martina","family":"Pohl","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jochen","family":"B\u00fcchs","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Antje C.","family":"Spiess","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2009,5,18]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1007\/BF01023952"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1097-0290(19960320)49:6<700::AID-BIT12>3.0.CO;2-9"},{"key":"e_1_2_1_4_2","doi-asserted-by":"publisher","DOI":"10.1039\/b405869k"},{"key":"e_1_2_1_5_2","doi-asserted-by":"crossref","unstructured":"Drapon R. 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