{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,11]],"date-time":"2025-11-11T13:13:03Z","timestamp":1762866783599},"reference-count":37,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2016,2,1]],"date-time":"2016-02-01T00:00:00Z","timestamp":1454284800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biotechnology"],"published-print":{"date-parts":[[2016,2]]},"DOI":"10.1016\/j.jbiotec.2015.12.034","type":"journal-article","created":{"date-parts":[[2015,12,28]],"date-time":"2015-12-28T16:47:05Z","timestamp":1451321225000},"page":"142-148","update-policy":"http:\/\/dx.doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":17,"special_numbering":"C","title":["Efficient cascade synthesis of ampicillin from penicillin G potassium salt using wild and mutant penicillin G acylase from Alcaligenes faecalis"],"prefix":"10.1016","volume":"219","author":[{"given":"Senwen","family":"Deng","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xiaoqiang","family":"Ma","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Erzheng","family":"Su","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dongzhi","family":"Wei","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbiotec.2015.12.034_bib0005","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1042\/bj20011468","article-title":"Role of \u03b1 Arg (145) and \u03b2 Arg (263) in the active site of penicillin acylase of E. coli","volume":"365","author":"Alkema","year":"2002","journal-title":"Biochem. J."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0010","doi-asserted-by":"crossref","first-page":"2093","DOI":"10.1046\/j.1432-1033.2002.02857.x","article-title":"The role of hydrophobic active-site residues in substrate specificity and acyltransfer activity of penicillin acylase","volume":"269","author":"Alkema","year":"2002","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0015","doi-asserted-by":"crossref","first-page":"23076","DOI":"10.1074\/jbc.M302246200","article-title":"The sequence and crystal structure of the \u03b1-amino acid ester hydrolase from Xanthomonas citri define a new family of \u03b2-lactam antibiotic acylases","volume":"278","author":"Barends","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0020","doi-asserted-by":"crossref","first-page":"1195","DOI":"10.1007\/s00253-013-4945-3","article-title":"Penicillin G acylase from Achromobacter sp. CCM 4824: an efficient biocatalyst for syntheses of beta-lactam antibiotics under conditions employed in large-scale processes","volume":"98","author":"Be\u010dka","year":"2014","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0025","doi-asserted-by":"crossref","first-page":"965","DOI":"10.1016\/0141-0229(93)90173-Y","article-title":"Synthesis of \u03b2-lactam antibiotics containing \u03b1-aminophenylacetyl group in the acyl moiety catalyzed by d-(\u2212)-phenylglycyl-\u03b2-lactamide amidohydrolase","volume":"15","author":"Blinkovsky","year":"1993","journal-title":"Enzyme Microb. Technol."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0030","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.molcatb.2010.06.014","article-title":"Amino ester hydrolase from Xanthomonas campestris pv. campestris, ATTC 33913 for enzymatic synthesis of ampicillin","volume":"67","author":"Blum","year":"2010","journal-title":"J. Mol. Catal. B Enzym."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0035","first-page":"987","article-title":"Ampicillin synthesis using a two-enzyme cascade with both \u03b1-amino ester hydrolase and penicillin G acylase","volume":"2","author":"Blum","year":"2010","journal-title":"Chem. Catal. Chem."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0040","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0045","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1021\/op9700643","article-title":"Penicillin acylase in the industrial production of \u03b2-lactam antibiotics","volume":"2","author":"Bruggink","year":"1998","journal-title":"Org. Process Res. Dev."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0050","volume":"335","author":"Bruggink","year":"2001"},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0055","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1007\/BF02932551","article-title":"Concentration of 6-aminopenicillanic acid from penicillin bioconversion solution and its mother liquor by nanofiltration membrane","volume":"6","author":"Cao","year":"2001","journal-title":"Biotechnol. Bioprocess Eng."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0060","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1023\/B:BILE.0000012885.62462.f3","article-title":"Production of 6-aminopenicillanic acid in aqueous two-phase systems by recombinant E. coli with intracellular penicillin acylase","volume":"26","author":"Cao","year":"2004","journal-title":"Biotechnol. Lett."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0065","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/j.enzmictec.2007.11.013","article-title":"The realm of penicillin G acylase in \u03b2-lactam antibiotics","volume":"42","author":"Chandel","year":"2008","journal-title":"Enzyme Microb. Technol."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0070","doi-asserted-by":"crossref","first-page":"1491","DOI":"10.1007\/s00253-011-3817-y","article-title":"Efficient biocatalyst for large-scale synthesis of cephalosporins, obtained by combining immobilization and site-directed mutagenesis of penicillin acylase","volume":"95","author":"Davide","year":"2012","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0075","series-title":"Ph.D. Thesis","author":"Deaguero","year":"2011"},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0080","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1093\/protein\/gzr065","article-title":"Improving the diastereoselectivity of penicillin G acylase for ampicillin synthesis from racemic substrates","volume":"25","author":"Deaguero","year":"2012","journal-title":"Protein Eng. Des. Sel."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0085","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1016\/j.jbiotec.2015.01.004","article-title":"Efficient enzymatic synthesis of ampicillin by mutant Alcaligenes faecalis penicillin G acylase","volume":"199","author":"Deng","year":"2015","journal-title":"J. Biotechnol."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0090","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1016\/j.molcatb.2008.12.020","article-title":"A two-step, one-pot enzymatic synthesis of ampicillin from penicillin G potassium salt","volume":"58","author":"Du","year":"2009","journal-title":"J. Mol. Catal. B Enzym."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0095","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1093\/protein\/gzh070","article-title":"Increasing the synthetic performance of penicillin acylase PAS2 by structure-inspired semi-random mutagenesis","volume":"17","author":"Gabor","year":"2004","journal-title":"Protein Eng. Des. Sel."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0100","doi-asserted-by":"crossref","first-page":"5398","DOI":"10.1016\/j.tetlet.2011.08.056","article-title":"Alcaligenes faecalis penicillin G acylase-catalyzed enantioselective acylation of dl-phenylalanine and derivatives in aqueous medium","volume":"52","author":"Gong","year":"2011","journal-title":"Tetrahedron Lett."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0105","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/j.enzmictec.2006.03.041","article-title":"Production of cephalexin in organic medium at high substrate concentrations with CLEA of penicillin acylase and PGA-450","volume":"40","author":"Illanes","year":"2007","journal-title":"Enzyme Microb. Technol."},{"issue":"1","key":"10.1016\/j.jbiotec.2015.12.034_bib0110","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1007\/BF00156291","article-title":"Evaluation of determination of 6-aminopenicillanic acid by p-dimethyl aminobenzaldedyde","volume":"1","author":"Jaiprakash","year":"1987","journal-title":"Biotechnol. Tech."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0115","doi-asserted-by":"crossref","first-page":"1335","DOI":"10.1016\/j.enzmictec.2006.10.014","article-title":"Hybrid penicillin acylases with improved properties for synthesis of beta-lactam antibiotics","volume":"40","author":"Jager","year":"2007","journal-title":"Enzyme Microb. Technol."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0120","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/j.jbiotec.2007.08.039","article-title":"Saturation mutagenesis reveals the importance of residues \u03b1R145 and \u03b1F146 of penicillin acylase in the synthesis of \u03b2-lactam antibiotics","volume":"133","author":"Jager","year":"2008","journal-title":"J. Biotechnol."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0125","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1002\/adsc.200505042","article-title":"Immobilization of penicillin G acylase: The key to optimum performance","volume":"347","author":"Kallenberg","year":"2005","journal-title":"Adv. Synth. Catal."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0130","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1016\/j.procbio.2008.04.024","article-title":"Characterization of smallest active monomeric penicillin V acylase from new source a yeast Rhodotorula aurantiaca (NCIM 3425)","volume":"43","author":"Kumar","year":"2008","journal-title":"Process Biochem."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0135","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1016\/S0734-9750(00)00039-2","article-title":"Advances in enzymatic transformation of penicillins to 6-aminopenicillanic acid (6-APA)","volume":"18","author":"Parmar","year":"2000","journal-title":"Biotechnol. Adv."},{"issue":"8\u20139","key":"10.1016\/j.jbiotec.2015.12.034_bib0140","doi-asserted-by":"crossref","first-page":"498","DOI":"10.1016\/S0141-0229(98)00140-9","article-title":"Thermodynamically controlled synthesis of \u03b2-lactam antibiotics: Equilibrium concentrations and side-chain properties","volume":"24","author":"Schro\u00ebn","year":"1999","journal-title":"Enzyme Microb. Technol."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0145","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1002\/bit.10348","article-title":"Integrated reactor concepts for the enzymatic kinetic synthesis of cephalexin","volume":"80","author":"Schro\u00ebn","year":"2002","journal-title":"Biotechnol. Bioeng."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0150","doi-asserted-by":"crossref","first-page":"3352","DOI":"10.1039\/b803584a","article-title":"E factors, green chemistry and catalysis: an odyssey","volume":"29","author":"Sheldon","year":"2008","journal-title":"Chem. Commun."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0155","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1016\/S0141-0229(96)00176-7","article-title":"Penicillin V acylase: its potential in the production of 6-amino penicillanic acid","volume":"20","author":"Shewale","year":"1997","journal-title":"Enzyme Microb. Technol."},{"issue":"8","key":"10.1016\/j.jbiotec.2015.12.034_bib0160","doi-asserted-by":"crossref","first-page":"1319","DOI":"10.1016\/j.biotechadv.2013.05.006","article-title":"Biotechnological advances on penicillin G acylase: pharmaceutical implications, unique expression mechanism and production strategies","volume":"31","author":"Srirangan","year":"2013","journal-title":"Biotechnol. Adv."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0165","doi-asserted-by":"crossref","first-page":"414","DOI":"10.1016\/S0014-5793(97)01289-1","article-title":"Kinetic study of penicillin acylase from Alcaligenes faecalis","volume":"417","author":"\u0160vedas","year":"1997","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0170","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1007\/s00253-006-0349-y","article-title":"Enhancing enzymatic activity of penicillin G acylase by coexpressing pcm gene","volume":"72","author":"Wang","year":"2006","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0175","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1002\/1615-4169(200108)343:6\/7<559::AID-ADSC559>3.0.CO;2-Z","article-title":"Towards biocatalytic synthesis of beta-lactam antibiotics","volume":"343","author":"Wegman","year":"2001","journal-title":"Adv. Synth. Catal."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0180","doi-asserted-by":"crossref","first-page":"2026","DOI":"10.1007\/s12010-009-8847-x","article-title":"Enzymatic synthesis of amoxicillin via a one-pot enzymatic hydrolysis and condensation cascade process in the presence of organic co-solvents","volume":"160","author":"Wu","year":"2010","journal-title":"Appl. Biochem. Biotechnol."},{"key":"10.1016\/j.jbiotec.2015.12.034_bib0185","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1007\/s00253-010-2727-8","article-title":"One-pot: two-step enzymatic synthesis of amoxicillin by complexing with Zn2+","volume":"88","author":"Zhang","year":"2010","journal-title":"Appl. Microbiol. Biotechnol."}],"container-title":["Journal of Biotechnology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0168165615302340?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0168165615302340?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2018,9,16]],"date-time":"2018-09-16T15:22:35Z","timestamp":1537111355000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0168165615302340"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,2]]},"references-count":37,"alternative-id":["S0168165615302340"],"URL":"https:\/\/doi.org\/10.1016\/j.jbiotec.2015.12.034","relation":{},"ISSN":["0168-1656"],"issn-type":[{"value":"0168-1656","type":"print"}],"subject":[],"published":{"date-parts":[[2016,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Efficient cascade synthesis of ampicillin from penicillin G potassium salt using wild and mutant penicillin G acylase from Alcaligenes faecalis","name":"articletitle","label":"Article Title"},{"value":"Journal of Biotechnology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbiotec.2015.12.034","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2015 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}