{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,15]],"date-time":"2026-09-15T15:52:43Z","timestamp":1789487563417,"version":"build-2803163510"},"reference-count":54,"publisher":"American Chemical Society (ACS)","issue":"36","license":[{"start":{"date-parts":[[2026,8,28]],"date-time":"2026-08-28T00:00:00Z","timestamp":1787875200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["JP 23K26470"],"award-info":[{"award-number":["JP 23K26470"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["JP 26K01319"],"award-info":[{"award-number":["JP 26K01319"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,9,15]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Controlled chemical conjugation of enzymes to the external surface of liposomes as simple biomembrane model systems and the investigation of the catalytic activity of such liposome-bound enzymes in vitro is one of the approaches toward a better understanding of enzymatic transformations occurring at biointerfaces in vivo. Liposomes with surface-bound enzymes may also find applications as soft, biodegradable immobilized enzyme systems for reactions carried out under mild conditions in an aqueous medium. In the present work, phosphoenolpyruvate carboxylase from microorganisms (PEPC) modified with 6-hydrazinonicotinate acetone hydrazone (PEPC-HyNic) was conjugated at 25 \u00b0C and pH = 7 to liposomes of about 100 nm diameter modified with 4-formylbenzoate (liposome-4FB) via the bis-aryl hydrazone (BAH) bond that forms upon reaction of HyNic with 4FB. The BAH bond formation and colloidal stability were followed for a dispersion of liposome-4FB reacting with PEPC-HyNic through monitoring of the time-dependent changes of the UV\/vis absorption spectrum, yielding catalytically active liposome-BAH-PEPC after chromatographic purification. Using the previously elaborated conditions for the preparation of (i) HyNic-modified bovine carbonic anhydrase (BCA-HyNic) and (ii) liposomes with surface-bound BCA (liposome-BAH-BCA), in the present work, liposomes containing both enzymes, BAH-bonded PEPC as well as BAH-bonded BCA, were prepared by sequentially attaching the two enzymes to the liposomes. For this, two approaches were applied. In the first approach, PEPC was first attached to the liposomes, followed by the attachment of BCA, yielding liposome-BAH-PEPC1\u00b7BCA2. In the second approach, BCA was first attached, followed by PEPC, yielding liposome-BAH-BCA1\u00b7PEPC2. For comparison, both enzymes were also attached simultaneously, yielding liposome-BAH-(PEPC\u00b7BCA). All three types of liposomes were characterized in terms of activity and stability of the two enzymes. The most successful approach turned out to be the one in which PEPC was attached first to the liposomes, liposome-BAH-PEPC1\u00b7BCA2. For the elaborated experimental conditions, each outer liposome surface contained on average about 2\u20133 active PEPC and about 100 active BCA molecules.<\/jats:p>","DOI":"10.1021\/acsomega.6c04259","type":"journal-article","created":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T04:50:37Z","timestamp":1788324637000},"page":"54053-54067","source":"Crossref","is-referenced-by-count":0,"title":["Sequential Conjugation\nof Two Different Types of Catalytically\nActive Enzymes to Liposomes via Bis-Aryl Hydrazone Bonds"],"prefix":"10.1021","volume":"11","author":[{"given":"Shungo","family":"Kotani","sequence":"first","affiliation":[{"name":"Yamaguchi University , , Tokiwadai 2-16-1 , ,","place":["Ube, Japan, 755-8611"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0827-0545","authenticated-orcid":true,"given":"Peter","family":"Walde","sequence":"additional","affiliation":[{"name":"ETH Zu\u0308rich , , Leopold-Ruzicka-Weg 4 , ,","place":["Zu\u0308rich, Switzerland, CH-8093"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7489-229X","authenticated-orcid":true,"given":"Makoto","family":"Yoshimoto","sequence":"additional","affiliation":[{"name":"Yamaguchi University , , Tokiwadai 2-16-1 , ,","place":["Ube, Japan, 755-8611"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,8,28]]},"reference":[{"key":"2026091510095127500_cit1","doi-asserted-by":"publisher","first-page":"3352","DOI":"10.1039\/b803584a","article-title":"E factors,\ngreen chemistry and catalysis: an odyssey","author":"Sheldon","year":"2008","journal-title":"Chem.\nCommun."},{"key":"2026091510095127500_cit2","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-025-63341-1","article-title":"Modular multi-enzyme\ncascades enable green and sustainable synthesis of non-canonical amino\nacids from glycerol","volume":"16","author":"Xu","year":"2025","journal-title":"Nat. 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Bioeng."},{"key":"2026091510095127500_cit6","doi-asserted-by":"publisher","first-page":"7910","DOI":"10.1021\/acs.jafc.1c02056","article-title":"Construction of multienzyme\nco-immobilized hybrid nanoflowers for an efficient conversion of cellulose\ninto glucose in a cascade reaction","volume":"69","author":"Han","year":"2021","journal-title":"J. Agric.\nFood Chem."},{"key":"2026091510095127500_cit7","doi-asserted-by":"publisher","first-page":"5481","DOI":"10.1021\/acs.langmuir.2c00053","article-title":"Co-immobilization\nof cellulase and\n\u03b2-glucosidase into mesoporous silica nanoparticles for the hydrolysis\nof cellulose extracted from Eriobotrya japonica leaves","volume":"38","author":"Pota","year":"2022","journal-title":"Langmuir"},{"key":"2026091510095127500_cit8","doi-asserted-by":"publisher","first-page":"169","DOI":"10.1016\/0956-5663(95)96804-8","article-title":"Cascade-like\nexponential substrate amplification in enzyme sensors","volume":"10","author":"Pfeiffer","year":"1995","journal-title":"Biosens. 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Interfaces"},{"key":"2026091510095127500_cit31","doi-asserted-by":"publisher","first-page":"949","DOI":"10.1038\/pj.2011.93","article-title":"Construction\nof a densely poly(ethylene glycol)-chain-tethered surface and its\nperformance","volume":"43","author":"Nagasaki","year":"2011","journal-title":"Polym. J."},{"key":"2026091510095127500_cit32","doi-asserted-by":"publisher","first-page":"18637","DOI":"10.1021\/acsomega.3c00551","article-title":"Preparation and catalytic properties\nof carbonic anhydrase conjugated to liposomes through a bis-aryl hydrazone\nbond","volume":"8","author":"Nagata","year":"2023","journal-title":"ACS Omega"},{"key":"2026091510095127500_cit33","doi-asserted-by":"publisher","first-page":"134","DOI":"10.1021\/bm101074s","article-title":"Preparation of catalytically\nactive, covalent \u03b1-polylysine-enzyme conjugates via UV\/Vis-quantifiable\nbis-aryl hydrazone bond formation","volume":"12","author":"Grotzky","year":"2011","journal-title":"Biomacromolecules"},{"key":"2026091510095127500_cit34","doi-asserted-by":"publisher","first-page":"445","DOI":"10.1016\/bs.mie.2017.01.014","article-title":"Preparation and applications\nof dendronized polymer-enzyme conjugates","volume":"590","author":"Ku\u0308chler","year":"2017","journal-title":"Methods\nEnzymol."},{"key":"2026091510095127500_cit35","doi-asserted-by":"publisher","first-page":"11392","DOI":"10.1021\/ja304837f","article-title":"A fluorescently labeled dendronized polymer-enzyme conjugate carrying\nmultiple copies of two different types of active enzymes","volume":"134","author":"Grotzky","year":"2012","journal-title":"J. Am. Chem. Soc."},{"key":"2026091510095127500_cit36","doi-asserted-by":"publisher","first-page":"44530","DOI":"10.1039\/C5RA06268C","article-title":"Enzyme immobilization on silica glass through simple adsorption of\ndendronized polymer-enzyme conjugates for localized enzymatic cascade\nreactions","volume":"5","author":"Ku\u0308chler","year":"2015","journal-title":"RSC Adv."},{"key":"2026091510095127500_cit37","doi-asserted-by":"publisher","first-page":"10391","DOI":"10.1021\/acsomega.8b01517","article-title":"Immobilization\nof carbonic anhydrase in glass micropipettes and glass fiber filters\nfor flow-through reactor applications","volume":"3","author":"Yoshimoto","year":"2018","journal-title":"ACS Omega"},{"key":"2026091510095127500_cit38","doi-asserted-by":"publisher","first-page":"1192","DOI":"10.1016\/0022-2836(92)90531-N","article-title":"Structure of native\nand apo carbonic anhydrase II and structure of some of its anion-ligand\ncomplexes","volume":"227","author":"H\u00e5kansson","year":"1992","journal-title":"J. Mol. Biol."},{"key":"2026091510095127500_cit39","doi-asserted-by":"publisher","first-page":"946","DOI":"10.1021\/cr050262p","article-title":"Carbonic\nanhydrase as a model for\nbiophysical and physical-organic studies of proteins and protein-ligand\nbinding","volume":"108","author":"Krishnamurthy","year":"2008","journal-title":"Chem. Rev."},{"key":"2026091510095127500_cit40","doi-asserted-by":"publisher","first-page":"2405","DOI":"10.1016\/S0021-9258(18)96634-2","article-title":"The enzymatic carboxylation\nof phosphoenolpyruvate. I. Purification and properties of phosphoenolpyruvate\ncarboxylase","volume":"241","author":"Maruyama","year":"1966","journal-title":"J. Biol. Chem."},{"key":"2026091510095127500_cit41","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/0014-5793(87)81454-0","article-title":"Higher\nplant phosphoenolpyruvate carboxylase. Structure\nand regulation","volume":"213","author":"Andreo","year":"1987","journal-title":"FEBS Lett."},{"key":"2026091510095127500_cit42","doi-asserted-by":"publisher","first-page":"25970","DOI":"10.1021\/acsami.5b09301","article-title":"Stable and\nsimple immobilization of proteinase K inside glass tubes and microfluidic\nchannels","volume":"7","author":"Ku\u0308chler","year":"2015","journal-title":"ACS Appl. Mater. Interfaces"},{"key":"2026091510095127500_cit43","doi-asserted-by":"publisher","DOI":"10.1002\/mabi.202200465","article-title":"Performance of a flow-through\nenzyme reactor prepared from a silica\nmonolith and an \u03b1-poly(D-lysine)-enzyme conjugate","volume":"23","author":"Ghe\u0301czy","year":"2023","journal-title":"Macromol. Biosci."},{"key":"2026091510095127500_cit44","unstructured":"For the properties of PEPC (PPC-301 from\nTOYOBO), see\n          2025\n          https:\/\/www.toyobo-global.com\/seihin\/xr\/enzyme\/enzyme_list\/PPC_301\/index.html."},{"key":"2026091510095127500_cit45","unstructured":"For the Safety Data Sheet (SDS No. 904F,\nfirst issue: May 1, 2014,\nrevised May 31, 2022) for PEPC (PPC-301 from TOYOBO), see\n          2026\n          https:\/\/www.toyobo-global.com\/seihin\/xr\/enzyme\/pdf\/package\/PPC-301.pdf."},{"key":"2026091510095127500_cit46","doi-asserted-by":"publisher","first-page":"539","DOI":"10.1093\/jxb\/29.3.539","article-title":"Phosphoenolpyruvate\ncarboxylase from Mesembryanthemum crystallinum: Its isolation and inactivation in vitro","volume":"29","author":"Winter","year":"1978","journal-title":"J. Exp. Botany"},{"key":"2026091510095127500_cit47","doi-asserted-by":"publisher","first-page":"823","DOI":"10.1073\/pnas.96.3.823","article-title":"Three-dimensional\nstructure if phosphoenolpyruvate carboxylase: A proposed\nmechanism for allosteric inhibition","volume":"96","author":"Kai","year":"1999","journal-title":"Proc. Natl.\nAcad. Sci. U. S. A."},{"key":"2026091510095127500_cit48","doi-asserted-by":"publisher","first-page":"792","DOI":"10.1107\/S0907444904003166","article-title":"Structure of bovine\ncarbonic anhydrase II at 1.95 \u00c5 resolution","volume":"60","author":"Saito","year":"2004","journal-title":"Acta Crystallogr., Sect. D:Biol. Crystallogr."},{"key":"2026091510095127500_cit49","unstructured":"For the properties of MDH (MDH-221 from\nTOYOBO), see\n          2025\n          https:\/\/www.toyobo-global.com\/seihin\/xr\/enzyme\/enzyme_list\/MAD_211\/index.html."},{"key":"2026091510095127500_cit50","doi-asserted-by":"publisher","first-page":"55","DOI":"10.1016\/0005-2736(85)90521-8","article-title":"Production of large\nunilamellar vesicles by a rapid procedure. Characterization of size\ndistribution, trapped volume and ability to maintain a membrane potential","volume":"812","author":"Hope","year":"1985","journal-title":"Biochim. Biophys. Acta"},{"key":"2026091510095127500_cit51","doi-asserted-by":"publisher","first-page":"297","DOI":"10.1016\/0005-2736(91)90295-J","article-title":"Small-volume extrusion apparatus\nfor preparation of large, unilamellar vesicles","volume":"1061","author":"MacDonald","year":"1991","journal-title":"Biochim. Biophys. Acta"},{"key":"2026091510095127500_cit52","unstructured":"For the properties of 4FB, see\n          2025\n          https:\/\/prod-vector-labs-wordpress-media.s3.amazonaws.com\/productattachments\/protocol\/VL_S-1004_UserGuide_LBL02183.pdf."},{"key":"2026091510095127500_cit53","doi-asserted-by":"publisher","first-page":"288","DOI":"10.1016\/0076-6879(69)13050-5","article-title":"Phosphoenolpyruvate\ncarboxylase from Escherichia coli","volume":"13","author":"Ca\u0301novas","year":"1969","journal-title":"Methods Enzymol."},{"key":"2026091510095127500_cit54","doi-asserted-by":"publisher","first-page":"159","DOI":"10.1016\/S0304-4157(00)00016-2","article-title":"Structure of lipid bilayers","volume":"1469","author":"Nagle","year":"2000","journal-title":"Biochim. Biophys. Acta"}],"container-title":["ACS Omega"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acsomega.6c04259","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/acsodf\/article-pdf\/11\/36\/54053\/67618463\/acsomega.6c04259.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/acsodf\/article-pdf\/11\/36\/54053\/67618463\/acsomega.6c04259.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,15]],"date-time":"2026-09-15T14:49:58Z","timestamp":1789483798000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/acsodf\/article\/11\/36\/54053\/5350537\/Sequential-Conjugation-of-Two-Different-Types-of"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8,28]]},"references-count":54,"journal-issue":{"issue":"36","published-online":{"date-parts":[[2026,8,28]]},"published-print":{"date-parts":[[2026,9,15]]}},"URL":"https:\/\/doi.org\/10.1021\/acsomega.6c04259","relation":{},"ISSN":["2470-1343"],"issn-type":[{"value":"2470-1343","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,8,28]]}}}