{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,2]],"date-time":"2025-11-02T19:46:42Z","timestamp":1762112802524,"version":"build-2065373602"},"reference-count":28,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2008,9,5]],"date-time":"2008-09-05T00:00:00Z","timestamp":1220572800000},"content-version":"vor","delay-in-days":2439,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biotechnology Progress"],"published-print":{"date-parts":[[2002,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Commercially available proteases and lipases were screened for their ability to acylate regioselectively sucrose with divinyladipate either in pyridine or dimethylformamide (DMF). The protease (EC 3.4.21.62) from\n                    <jats:italic>Bacillus subtilis<\/jats:italic>\n                    (Proleather FG\u2010F) exhibited the highest conversion (100% in 24 h of reaction in DMF) yielding sucrose 2\u2010\n                    <jats:italic>O<\/jats:italic>\n                    \u2010vinyladipate as main product. The enzyme preference for a secondary hydroxyl group is a distinct feature of this biocatalyst compared to others described in the literature. Two sets of chemically distinct silica supports were used for Proleather immobilization presenting terminal amino (S\n                    <jats:sub>APTES<\/jats:sub>\n                    ) or hydroxyl groups (S\n                    <jats:sub>TESPM<\/jats:sub>\n                    <jats:sub>\u2010<\/jats:sub>\n                    <jats:sub>pHEMA<\/jats:sub>\n                    ). The percentage of immobilized enzyme was smaller in S\n                    <jats:sub>APTES<\/jats:sub>\n                    (7\u201317%) than in S\n                    <jats:sub>TESPM<\/jats:sub>\n                    <jats:sub>\u2010<\/jats:sub>\n                    <jats:sub>pHEMA<\/jats:sub>\n                    (52\u201356%), yet Proleather immobilized into S\n                    <jats:sub>APTES<\/jats:sub>\n                    supports presented higher total and specific hydrolytic activity. The highest total and specific activities were obtained with S\n                    <jats:sub>TESPM<\/jats:sub>\n                    <jats:sub>\u2010<\/jats:sub>\n                    <jats:sub>pHEMA<\/jats:sub>\n                    and S\n                    <jats:sub>APTES<\/jats:sub>\n                    , respectively. Silicas with large pore (bimodal distribution of pores, 130\/1200 \u00c5, denoted as S\n                    <jats:sub>1000<\/jats:sub>\n                    ) presented higher specific activities relative to those with smaller pore sizes. Furthermore, the synthetic specific activity of S\n                    <jats:sub>1000<\/jats:sub>\n                    S\n                    <jats:sub>APTES<\/jats:sub>\n                    immobilized protease was ca. 10\u2010fold higher than that of the free enzyme. In addition to sucrose, the immobilized protease was used to acylate methyl \u03b1\u2010\n                    <jats:sc>d<\/jats:sc>\n                    \u2010glucopyranoside, trehalose, and maltose in nearly anhydrous DMF. Finally, immobilized Proleather was reasonably stable, retaining ca. 55% activity after six reaction cycles.\n                  <\/jats:p>","DOI":"10.1021\/bp0255457","type":"journal-article","created":{"date-parts":[[2002,10,4]],"date-time":"2002-10-04T00:33:03Z","timestamp":1033691583000},"page":"986-993","source":"Crossref","is-referenced-by-count":15,"title":["Exquisite Regioselectivity and Increased Transesterification Activity of an Immobilized\n                    <i>Bacillus subtilis<\/i>\n                    Protease"],"prefix":"10.1002","volume":"18","author":[{"given":"Lino","family":"Ferreira","sequence":"first","affiliation":[]},{"given":"M. A.","family":"Ramos","sequence":"additional","affiliation":[]},{"given":"Maria Helena","family":"Gil","sequence":"additional","affiliation":[]},{"given":"Jonathan S.","family":"Dordick","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2008,9,5]]},"reference":[{"key":"e_1_2_7_2_2","doi-asserted-by":"publisher","DOI":"10.1002\/macp.1996.021970120"},{"key":"e_1_2_7_3_2","first-page":"265","volume-title":"Sucrose: Properties and applications","author":"Khan R.","year":"1995"},{"key":"e_1_2_7_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0144-8617(99)00064-8"},{"key":"e_1_2_7_5_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja00278a053"},{"key":"e_1_2_7_6_2","doi-asserted-by":"publisher","DOI":"10.1021\/ma00122a005"},{"key":"e_1_2_7_7_2","doi-asserted-by":"publisher","DOI":"10.1021\/ma00052a001"},{"key":"e_1_2_7_8_2","doi-asserted-by":"publisher","DOI":"10.1021\/ma00011a068"},{"key":"e_1_2_7_9_2","doi-asserted-by":"publisher","DOI":"10.1002\/bit.260370706"},{"key":"e_1_2_7_10_2","doi-asserted-by":"publisher","DOI":"10.1002\/1097-0290(20001020)70:2<208::AID-BIT10>3.0.CO;2-0"},{"key":"e_1_2_7_11_2","doi-asserted-by":"publisher","DOI":"10.3109\/10242429909015219"},{"key":"e_1_2_7_12_2","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1097-0290(19991005)65:1<10::AID-BIT2>3.0.CO;2-L"},{"key":"e_1_2_7_13_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0141-0229(96)00067-1"},{"key":"e_1_2_7_14_2","doi-asserted-by":"publisher","DOI":"10.1021\/cm9708123"},{"key":"e_1_2_7_15_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0032-5910(98)00061-8"},{"key":"e_1_2_7_16_2","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(77)90428-6"},{"key":"e_1_2_7_17_2","doi-asserted-by":"crossref","first-page":"2930","DOI":"10.1016\/S0021-9258(19)76404-7","article-title":"The spectrophotometric determination of the operational normality of an \u03b1\u2010chymotrypsin solution","volume":"236","author":"Schonbaum G. R.","year":"1961","journal-title":"J. Biol. Chem."},{"key":"e_1_2_7_18_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja00210a045"},{"key":"e_1_2_7_19_2","doi-asserted-by":"publisher","DOI":"10.1248\/cpb.28.2065"},{"key":"e_1_2_7_20_2","doi-asserted-by":"crossref","unstructured":"Carrea G.;Riva S.;Secundo F.;Danieli B.Enzymatic synthesis of various 1\u2032\u2010O\u2010sucrose and 1\u2010O\u2010fructose esters.J. Chem. Soc. Perkin Trans. 11989 1057\u20131061.","DOI":"10.1039\/P19890001057"},{"key":"e_1_2_7_21_2","doi-asserted-by":"publisher","DOI":"10.3109\/10242429408998144"},{"key":"e_1_2_7_22_2","doi-asserted-by":"publisher","DOI":"10.1002\/bit.260450507"},{"key":"e_1_2_7_23_2","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1097-0290(19980105)57:1<121::AID-BIT15>3.0.CO;2-N"},{"key":"e_1_2_7_24_2","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1097-0290(19960205)49:3<328::AID-BIT11>3.0.CO;2-A"},{"key":"e_1_2_7_25_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja00247a024"},{"key":"e_1_2_7_26_2","first-page":"103","volume-title":"Biochemical Enginnering","author":"Blanch H. W.","year":"1996"},{"key":"e_1_2_7_27_2","unstructured":"Calculations of values of observable modulus(\u03a6)are based on a radius of the silica particles of 15 (S300STESPM\u2010pHEMA) and 14.5 \u03bcm (S1000STESPM\u2010pHEMA) a bulk substrate concentration of 0.28 mM andDeff(for \u03b8 = 7.0) of 2.28 \u00d7 10\u22127(S300STESPM\u2010pHEMA) and 2.39 \u00d7 10\u22127cm2s\u22121(S1000STESPM\u2010pHEMA). The hindrance factor (H) was not included in the calculations since the radius of the pore (<170 \u00c5) is much greater than that of the solute molecule (\u224520 \u00c5 considering that casein is a globular protein). Furthermore the bulk diffusivity (Ds) was calculated from the Stokes Einstein equation (see ref 25) and was 2.1 \u00d7 10\u22126cm2s\u22121."},{"key":"e_1_2_7_28_2","doi-asserted-by":"publisher","DOI":"10.1002\/jctb.280580105"},{"key":"e_1_2_7_29_2","doi-asserted-by":"publisher","DOI":"10.1021\/bp00016a001"}],"container-title":["Biotechnology Progress"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1021%2Fbp0255457","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/aiche.onlinelibrary.wiley.com\/doi\/pdf\/10.1021\/bp0255457","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,27]],"date-time":"2025-10-27T10:45:20Z","timestamp":1761561920000},"score":1,"resource":{"primary":{"URL":"https:\/\/aiche.onlinelibrary.wiley.com\/doi\/10.1021\/bp0255457"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2002,1]]},"references-count":28,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2002,1]]}},"alternative-id":["10.1021\/bp0255457"],"URL":"https:\/\/doi.org\/10.1021\/bp0255457","archive":["Portico"],"relation":{},"ISSN":["8756-7938","1520-6033"],"issn-type":[{"type":"print","value":"8756-7938"},{"type":"electronic","value":"1520-6033"}],"subject":[],"published":{"date-parts":[[2002,1]]}}}