375:
have been found to greatly increase the maximum resistance and decrease extensibility of the dough. The resistance was increased due to the crosslinking of AX via ferulic acid and resulting in a strong AX and gluten network. Although laccase is known to crosslink AX, under the microscope it was found that the laccase also acted on the flour proteins. Oxidation of the ferulic acid on AX to form ferulic acid radicals increased the oxidation rate of free SH groups on the gluten proteins and thus influenced the formation of S-S bonds between gluten polymers. Laccase is also able to oxidize peptide-bound tyrosine, but very poorly. Because of the increased strength of the dough, it showed irregular bubble formation during proofing. This was a result of the gas (carbon dioxide) becoming trapped within the crust so it could not diffuse out (like it would have normally) and causing abnormal pore size. Resistance and extensibility was a function of dosage, but at very high dosage the dough showed contradictory results: maximum resistance was reduced drastically. The high dosage may have caused extreme changes in the structure of dough, resulting in incomplete gluten formation. Another reason is that it may mimic overmixing, causing negative effects on gluten structure. Laccase-treated dough had low stability over prolonged storage. The dough became softer and this is related to laccase mediation. The laccase-mediated radical mechanism creates secondary reactions of FA-derived radicals that result in breaking of covalent linkages in AX and weakening of the AX gel.
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Laccases have the potential to crosslink food polymers such as proteins and nonstarch polysaccharides in dough. In non-starch polysaccharides, such as arabinoxylans (AX), laccase catalyzes the oxidative gelation of feruloylated arabinoxylans by dimerization of their ferulic esters. These cross-links
393:
Pers. (1794). Laccase is active at wine pH and its activity is not readily suppressed by sulfur dioxide. It has been noted to cause oxidative browning in white wines and loss of colour in red wines. It can also degrade a number of key phenolic compounds critical to wine quality. Aside from wine,
350:
removes all copper from the enzyme, and re-embedding with type I and type II copper has been shown to be impossible. Type III copper, however, can be re-embedded back into the enzyme. A variety of other anions inhibit laccase.
1034:
Zimdars S, Hitschler J, Schieber A, Weber F (2017). "Oxidation of wine polyphenols by secretomes of wild
Botrytis cinerea strains from white and red grape varieties and determination of their specific laccase activity".
946:
Zimdars S, Hitschler J, Schieber A, Weber F (2017). "Oxidation of wine polyphenols by secretomes of wild
Botrytis cinerea strains from white and red grape varieties and determination of their specific laccase activity".
317:
The active site consists of four copper centers, which adopt structures classified as type I, type II, and type III. A tricopper ensemble contains types II and III copper (see figure). It is this center that binds
342:. The final copper center is the type II copper center, which has two histidine ligands and a hydroxide ligand. The type II together with the type III copper center forms the tricopper ensemble, which is where
366:. They can be paired with an electron mediator to facilitate electron transfer to a solid electrode wire. Laccases are some of the few oxidoreductases commercialized as industrial catalysts.
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Vignault A, Pascual O, Jourdes M, Moine V, Fermaud M, Roudet J, Canals JM, Teissedre PL, Zamora F (2019). "Impact of enological tannins on laccase activity".
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ligand. The type III copper center consists of two copper atoms that each possess three histidine ligands and are linked to one another via a hydroxide
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326:, but functions solely as an electron transfer site. The type I copper center consists of a single copper atom that is ligated to a minimum of two
919:
Minussi RC, Rossi M, Bologna L, Rotilio D, Pastore GM, Durán N (2007). "Phenols
Removal in Musts: Strategy for Wine Stabilization by Laccase".
1252:
865:
725:
491:
Cohen R, Persky L, Hadar Y (April 2002). "Biotechnological applications and potential of wood-degrading mushrooms of the genus
Pleurotus".
1882:
708:
Alcalde M (2007). "Laccases: Biological functions, molecular structure and industrial applications.". In
Polaina J, MacCabe AP (eds.).
1593:
884:
Selinheimo E, Autio K, Kruus K, Buchert J (July 2007). "Elucidating the mechanism of laccase and tyrosinase in wheat bread making".
792:"Bioelectrocatalytic hydrogels from electron-conducting metallopolypeptides coassembled with bifunctional enzymatic building blocks"
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and reduces it to water. Each Cu(I,II) couple delivers one electron required for this conversion. The type I copper does not bind O
405:
194:
145:
121:
1749:
1341:
Suresh PS, Kumar A, Kumar R, Singh VP (January 2008). "An in silico approach to bioremediation: laccase as a case study".
1164:
Monti, Daniela; Ottolina, Gianluca; Carrea, Giacomo; Riva, Sergio (2011). "Redox
Reactions Catalyzed by Isolated Enzymes".
334:
residue, but in some laccases produced by certain plants and bacteria, the type I copper center contains an additional
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reduction takes place. The type III copper can be replaced by Hg(II), which causes a decrease in laccase activity.
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Thorum MS, Anderson CA, Hatch JJ, Campbell AS, Marshall NM, Zimmerman SC, et al. (August 2010).
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The ability of laccases to modify complex organic molecules has attracted attention in the area of
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229:
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44:
1064:"Laccases in Food Industry: Bioprocessing, Potential Industrial and Biotechnological Applications"
66:
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743:"Direct, Electrocatalytic Oxygen Reduction by Laccase on Anthracene-2-methanethiol Modified Gold"
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1201:"Degradation of Pharmaceuticals and Personal Care Products by White-Rot Fungi—a Critical Review"
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Solomon EI, Sundaram UM, Machonkin TE (November 1996). "Multicopper
Oxidases and Oxygenases".
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1003:"Effects of laccase from Botrytis cinerea on the oxidative degradation of anthocyanins"
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Laccase is produced by a number of fungal species that can infect grapes, most notably
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536:"Unraveling Melanin Biosynthesis and Signaling Networks in Cryptococcus neoformans"
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Proceedings of the
National Academy of Sciences of the United States of America
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262:, play a role in the degradation of lignin, and can therefore be classed as
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Tschofen, Marc; Knopp, Dietmar; Hood, Elizabeth; Stöger, Eva (2016-06-12).
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Xu F (Spring 2005). "Applications of oxidoreductases: Recent progress".
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Tyrosinase and laccase as novel crosslinking tools for food biopolymers
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109:
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Lee D, Jang EH, Lee M, Kim SW, Lee Y, Lee KT, Bahn YS (October 2019).
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266:. Other laccases produced by fungi can facilitate the biosynthesis of
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Laccase was first studied by
Hikorokuro Yoshida in 1883 and then by
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found in plants, fungi, and bacteria. Laccases oxidize a variety of
1806:
384:
292:
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pigments. Laccases catalyze ring cleavage of aromatic compounds.
1062:
Mayolo-Deloisa K, González-González M, Rito-Palomares M (2020).
1001:
Giménez P, Just-Borràs A, Gombau J, Canals JM, Zamora F (2023).
583:
Claus H (2004). "Laccases: structure, reactions, distribution".
97:
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1113:
Osma JF, Toca-Herrera JL, RodrĂguez-Couto S (September 2010).
790:
Wheeldon IR, Gallaway JW, Barton SC, Banta S (October 2008).
404:
Laccases have been also been studied as catalysts to degrade
1316:"Laccases for Denim Bleaching: An Eco-Friendly Alternative"
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297:
The tricopper site found in many laccases; note that each
635:
Science and civilisation in China: Chemistry and chemical
256:. Other laccases, such as those produced by the fungus
244:. For example, laccases play a role in the formation of
638:. Vol. 5. Cambridge University Press. p. 209.
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Asif MB, Hai FI, Singh L, Price WE, Nghiem LD (2017).
661:"Electron transfer and reaction mechanism of laccases"
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362:. The enzyme has been examined as the cathode in
394:laccases are of interest in the food industry.
383:Laccases have been applied in the production of
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1343:Journal of Molecular Graphics & Modelling
1068:Frontiers in Bioengineering and Biotechnology
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860:. VTT Technical Research Centre of Finland.
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1115:"Uses of laccases in the food industry"
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248:by promoting the oxidative coupling of
493:Applied Microbiology and Biotechnology
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1253:Annual Review of Analytical Chemistry
7:
1378:(1). Mary Ann Liebert, Inc.: 38–50.
1314:Rodriguez-Couto, S (February 2012).
1279:10.1146/annurev-anchem-071015-041706
665:Cellular and Molecular Life Sciences
632:Lu GD, Ho PY, Sivin N (1980-09-25).
236:substrates, performing one-electron
1504:Coenzyme Q - cytochrome c reductase
659:Jones SM, Solomon EI (March 2015).
14:
1020:10.20870/oeno-one.2023.57.3.7567
988:10.20870/oeno-one.2019.53.1.2361
619:"Gabriel Bertrand on isimabomba"
422:
712:. Springer. pp. 461–476.
309:(color code: copper is brown,
1:
933:10.1016/j.molcatb.2006.12.004
854:Selinheimo E (October 2008).
379:Biotechnological applications
597:10.1016/j.micron.2003.10.029
1333:10.2174/1876520301205010001
254:naturally occurring phenols
1904:
1883:Natural phenols metabolism
1355:10.1016/j.jmgm.2007.05.005
285:, hence the name laccase.
277:in 1894 in the sap of the
1750:Michaelis–Menten kinetics
1225:10.1007/s40726-017-0049-5
1205:Current Pollution Reports
677:10.1007/s00018-014-1826-6
505:10.1007/s00253-002-0930-y
356:oxygen reduction reaction
281:, where it helps to form
167:
1642:Diffusion-limited enzyme
1424:Medical Subject Headings
1372:Industrial Biotechnology
1081:10.3389/fbioe.2020.00222
1049:10.1021/acs.jafc.7b04375
961:10.1021/acs.jafc.7b04375
718:10.1007/1-4020-5377-0_26
264:lignin-modifying enzymes
921:J. Mol. Catal. B: Enzym
817:10.1073/pnas.0805249105
370:Activity in wheat dough
364:enzymatic biofuel cells
301:center is bound to the
1545:Cytochrome b6f complex
330:residues and a single
314:
1735:Eadie–Hofstee diagram
1668:Allosteric regulation
1384:10.1089/ind.2005.1.38
552:10.1128/mBio.02267-19
354:Laccases affects the
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279:Japanese lacquer tree
1745:Lineweaver–Burk plot
1320:Open Textile Journal
230:multicopper oxidases
1561:Alternative oxidase
1270:2016ARAC....9..271T
1217:2017CPolR...3...88A
1132:10.4061/2010/918761
1037:J. Agric. Food Chem
949:J. Agric. Food Chem
808:2008PNAS..10515275W
802:(40): 15275–15280.
406:emerging pollutants
259:Pleurotus ostreatus
1704:Enzyme superfamily
1637:Enzyme promiscuity
710:Industrial Enzymes
429:Biology portal
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898:10.1021/jf0703349
892:(15): 6357–6365.
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470:10.1021/cr950046o
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275:Gabriel Bertrand
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1211:(2): 88–103.
1210:
1206:
1202:
1195:
1192:
1187:
1183:
1179:
1175:
1171:
1167:
1160:
1157:
1152:
1148:
1143:
1138:
1133:
1128:
1124:
1120:
1116:
1109:
1106:
1101:
1097:
1092:
1087:
1082:
1077:
1073:
1069:
1065:
1058:
1055:
1050:
1046:
1042:
1038:
1030:
1027:
1021:
1016:
1012:
1008:
1004:
997:
994:
989:
985:
981:
977:
970:
967:
962:
958:
954:
950:
942:
939:
934:
930:
926:
922:
915:
912:
907:
903:
899:
895:
891:
887:
880:
878:
874:
869:
863:
859:
858:
850:
848:
846:
842:
837:
833:
828:
823:
818:
813:
809:
805:
801:
797:
793:
786:
783:
778:
774:
769:
764:
760:
756:
752:
748:
744:
737:
734:
729:
723:
719:
715:
711:
704:
701:
696:
692:
687:
682:
678:
674:
670:
666:
662:
655:
652:
647:
645:9780521085731
641:
637:
636:
628:
625:
620:
614:
611:
606:
602:
598:
594:
590:
586:
579:
576:
571:
567:
562:
557:
553:
549:
545:
541:
537:
530:
527:
522:
518:
514:
510:
506:
502:
498:
494:
487:
484:
479:
475:
471:
467:
463:
459:
452:
450:
446:
439:
434:
430:
425:
420:
419:
415:
413:
411:
407:
402:
400:
395:
392:
391:
386:
378:
376:
369:
367:
365:
361:
357:
352:
349:
345:
341:
337:
333:
329:
312:
308:
304:
300:
295:
288:
286:
284:
280:
276:
271:
269:
265:
261:
260:
255:
251:
247:
243:
240:, leading to
239:
235:
231:
227:
224:
220:
208:
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203:
199:
196:
193:
191:
187:
184:
181:
179:
175:
170:
166:
163:
159:
156:
154:
153:Gene Ontology
150:
147:
144:
141:
138:
135:
131:
128:
125:
123:
119:
116:
113:
111:
107:
104:
101:
99:
95:
92:
91:NiceZyme view
89:
87:
83:
80:
77:
75:
71:
68:
65:
63:
59:
54:
51:
48:
46:
42:
39:
36:
34:
30:
25:
20:
1846:Translocases
1843:
1830:
1817:
1804:
1791:
1781:Transferases
1778:
1765:
1622:Binding site
1526:
1375:
1371:
1346:
1342:
1323:
1319:
1257:
1251:
1241:
1208:
1204:
1194:
1169:
1165:
1159:
1122:
1118:
1108:
1071:
1067:
1057:
1040:
1036:
1029:
1010:
1006:
996:
979:
975:
969:
952:
948:
941:
924:
920:
914:
889:
885:
856:
799:
795:
785:
750:
746:
736:
709:
703:
668:
664:
654:
634:
627:
621:(in French).
613:
588:
584:
578:
543:
539:
529:
496:
492:
486:
461:
457:
403:
396:
388:
382:
373:
353:
316:
272:
257:
242:crosslinking
218:
217:
79:BRENDA entry
1617:Active site
1264:: 271–294.
289:Active site
250:monolignols
67:IntEnz view
50:80498-15-3
27:Identifiers
1867:Categories
1820:Isomerases
1794:Hydrolases
1661:Regulation
1326:(1): 1–7.
1125:: 918761.
1074:(8): 222.
435:References
336:methionine
307:histidines
238:oxidations
136:structures
103:KEGG entry
1878:EC 1.10.3
1699:EC number
1392:1931-8421
1288:1936-1327
440:Citations
328:histidine
313:is blue).
303:imidazole
56:Databases
1888:Proteins
1723:Kinetics
1647:Cofactor
1610:Activity
1467:family (
1465:diphenol
1400:56165525
1363:17606396
1296:27049632
1233:51897758
1186:21526768
1151:21048873
1100:32266246
1007:OENO One
976:OENO One
906:17602567
836:18824691
777:20847902
695:25572295
605:15036303
570:31575776
521:45444911
513:11956739
478:11848837
416:See also
344:dioxygen
332:cysteine
311:nitrogen
234:phenolic
226:1.10.3.2
219:Laccases
207:proteins
195:articles
183:articles
140:RCSB PDB
38:1.10.3.2
1833:Ligases
1603:Enzymes
1537:1.10.99
1527:Laccase
1420:Laccase
1266:Bibcode
1213:Bibcode
1142:2963825
1091:7105568
827:2563127
804:Bibcode
768:2938065
686:4323859
561:6775464
358:at low
348:Cyanide
283:lacquer
268:melanin
162:QuickGO
127:profile
110:MetaCyc
45:CAS no.
22:Laccase
1807:Lyases
1514:1.10.3
1496:1.10.2
1478:1.10.1
1426:(MeSH)
1415:BRENDA
1398:
1390:
1361:
1294:
1286:
1231:
1184:
1149:
1139:
1098:
1088:
904:
864:
834:
824:
775:
765:
724:
693:
683:
642:
603:
585:Micron
568:
558:
519:
511:
476:
299:copper
246:lignin
228:) are
190:PubMed
172:Search
158:AmiGO
146:PDBsum
86:ExPASy
74:BRENDA
62:IntEnz
33:EC no.
1759:Types
1554:Other
1471:1.10)
1396:S2CID
1260:(1).
1229:S2CID
517:S2CID
385:wines
122:PRIAM
1851:list
1844:EC7
1838:list
1831:EC6
1825:list
1818:EC5
1812:list
1805:EC4
1799:list
1792:EC3
1786:list
1779:EC2
1773:list
1766:EC1
1388:ISSN
1359:PMID
1292:PMID
1284:ISSN
1182:PMID
1147:PMID
1123:2010
1096:PMID
902:PMID
862:ISBN
832:PMID
773:PMID
722:ISBN
691:PMID
640:ISBN
601:PMID
566:PMID
540:mBio
509:PMID
474:PMID
408:and
202:NCBI
143:PDBe
98:KEGG
1380:doi
1351:doi
1328:doi
1274:doi
1221:doi
1174:doi
1170:111
1137:PMC
1127:doi
1086:PMC
1076:doi
1045:doi
1015:doi
984:doi
957:doi
929:doi
894:doi
822:PMC
812:doi
800:105
763:PMC
755:doi
714:doi
681:PMC
673:doi
593:doi
556:PMC
548:doi
501:doi
466:doi
401:].
178:PMC
134:PDB
1869::
1469:EC
1463::
1394:.
1386:.
1374:.
1357:.
1347:26
1345:.
1322:.
1318:.
1290:.
1282:.
1272:.
1256:.
1250:.
1227:.
1219:.
1207:.
1203:.
1180:.
1168:.
1145:.
1135:.
1121:.
1117:.
1094:.
1084:.
1070:.
1066:.
1041:65
1039:.
1013:.
1011:57
1009:.
1005:.
982:.
980:53
978:.
953:65
951:.
925:45
923:.
900:.
890:55
888:.
876:^
844:^
830:.
820:.
810:.
798:.
794:.
771:.
761:.
749:.
745:.
720:.
689:.
679:.
669:72
667:.
663:.
599:.
589:35
587:.
564:.
554:.
544:10
542:.
538:.
515:.
507:.
497:58
495:.
472:.
462:96
460:.
448:^
412:.
223:EC
160:/
1853:)
1849:(
1840:)
1836:(
1827:)
1823:(
1814:)
1810:(
1801:)
1797:(
1788:)
1784:(
1775:)
1771:(
1595:e
1588:t
1581:v
1453:e
1446:t
1439:v
1402:.
1382::
1376:1
1365:.
1353::
1336:.
1330::
1324:5
1298:.
1276::
1268::
1258:9
1235:.
1223::
1215::
1209:3
1188:.
1176::
1153:.
1129::
1102:.
1078::
1072:8
1051:.
1047::
1023:.
1017::
990:.
986::
963:.
959::
935:.
931::
908:.
896::
870:.
838:.
814::
806::
779:.
757::
751:1
730:.
716::
697:.
675::
648:.
607:.
595::
572:.
550::
523:.
503::
480:.
468::
324:2
320:2
318:O
221:(
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