306:
enzyme can be seen in the first figure. The second figure shows the activity of the enzyme, and shows both cellulose binding to the enzyme, as well as the product of this step, cellobiose. Research suggests, however, that the activity of CBH1 is very strong inhibited by the product, cellobiose. Determination of an enzyme that is not as strongly inhibited by the product or finding a way to remove cellobiose from the environment of the enzyme are just more examples of the many challenges that face the use of these enzymes for the creation of biofuels.
1482:
310:
318:
37:
329:
Some notable improvements have been made in this area as well. For example, a strain of yeast capable of producing its own cellulose digesting enzyme has been developed, which would allow the cellulose degradation and the fermentation steps could be at once. This is an important development in the
305:
CBH1 from yeast, for example, is composed of a carbohydrate binding site, a linker region and a catalytic domain. Once the cellulose chain is bound, it is strung through a tunnel-shaped active site where the cellulose is broken down into two-sugar segments called cellobiose. The structure of the
325:
After above step, the process for creating ethanol is as follows: 3. Separation of sugars from other plant material. 4. Microbial fermentation of the sugar solution to create alcohol. 5. Distillation to purify the products and produce roughly 9% pure alcohol 6. Further purification to bring the
254:
The main technological impediment to widespread utilization of cellulose for fuels is still the lack of low-cost technologies to convert cellulose. One solution is the use of organisms that are capable of performing this conversion. Development of such organisms, such as
235:, exo-cellobiohydrolase, β-1,4-glucan cellobiohydrolase, β-1,4-glucan cellobiosylhydrolase, 1,4-β-glucan cellobiosidase, exoglucanase, avicelase, CBH 1, C1 cellulase, cellobiohydrolase I, cellobiohydrolase, exo-β-1,4-glucan cellobiohydrolase, 1,4-β-
351:
Ilmén M, den Haan R, Brevnova E, McBride J, Wiswall E, Froehlich A, Koivula A, Voutilainen SP, Siika-Aho M, la Grange DC, Thorngren N, Ahlgren S, Mellon M, Deleault K, Rajgarhia V, van Zyl WH, Penttilä M (September 2011).
652:
Du F, Wolger E, Wallace L, Liu A, Kaper T, Kelemen B (May 2010). "Determination of
Product Inhibition of CBH1, CBH2, and EG1 Using a Novel Cellulase Activity Assay".
189:
634:
208:
819:
695:
Zhu JY, Pan XJ, Wang GS, Gleisner R (April 2009). "Sulfite pretreatment (SPORL) for robust enzymatic saccharification of spruce and red pine".
259:
which is capable of secreting high levels of cellobiohydrolases, is already underway. Cellobiohydrolases are exoglucanases derived from fungi.
787:
1201:
201:
1083:
812:
168:
144:
1357:
1095:
1472:
730:
Galazka, Jonathan M.; Tian, Chaoguang; Beeson, William T.; Martinez, Bruno; Glass, N. Louise; Cate, Jamie H. D. (2010).
942:
1342:
1458:
1445:
1432:
1419:
1406:
1393:
1380:
1153:
841:
805:
1352:
465:
for the breakdown of cellulose. 3. Purification and physico-chemical characterization of an exo-1,4-β-glucanase"
162:
1306:
1249:
832:
791:
229:
55:
149:
1254:
1005:
1168:
913:
353:
213:
1275:
1194:
137:
1347:
553:
Zverlov VV, Velikodvorskaya GV, Schwarz WH, Bronnenmeier K, Kellermann J, Staudenbauer WL (June 1998).
72:
1127:
1078:
743:
321:
CBH1 zoomed in on the active site where cellulose is cleaved into cellobiose, generated using pymol.
1311:
1022:
1010:
845:
165:
67:
89:
1244:
1066:
1061:
1039:
1027:
866:
767:
677:
248:
1502:
1034:
908:
759:
712:
669:
588:
535:
486:
437:
412:"The mechanism of enzymatic cellulose degradation. Purification of a cellulolytic enzyme from
392:
156:
609:
1290:
1285:
1259:
1187:
1044:
930:
751:
704:
661:
578:
570:
525:
517:
476:
427:
382:
372:
125:
1337:
1321:
1234:
1164:
731:
263:
101:
747:
232:
60:
1486:
1375:
1316:
1105:
1017:
854:
797:
530:
505:
481:
456:
432:
411:
387:
184:
583:
554:
1496:
1280:
1239:
1051:
980:
963:
574:
771:
681:
1229:
895:
708:
295:
1453:
1388:
1224:
1122:
1088:
1056:
1481:
1132:
1100:
665:
299:
283:
1427:
1401:
970:
903:
880:
870:
828:
755:
309:
291:
279:
244:
17:
763:
716:
673:
610:"Cellulase Enzymes for the Conversion of Biomass to Biofuels and Chemicals"
396:
377:
317:
592:
539:
441:
975:
490:
521:
330:
sense that it makes large scale, industrial applications more feasible.
113:
958:
885:
875:
862:
132:
1440:
1210:
240:
196:
108:
96:
84:
1414:
1137:
918:
316:
308:
36:
732:"Cellodextrin Transport in Yeast for Improved Biofuel Production"
1115:
1110:
1071:
1000:
995:
990:
985:
935:
923:
120:
1183:
801:
555:"Multidomain structure and cellulosomal localization of the
1179:
1470:
788:
Cellulose+1,4-beta-cellobiosidase+(non-reducing+end)
457:"Extracellular enzyme system utilized by the fungus
1366:
1330:
1299:
1268:
1217:
1152:
951:
894:
853:
840:
506:"The role of component C 1 in cellulolytic systems"
207:
195:
183:
178:
155:
143:
131:
119:
107:
95:
83:
78:
66:
54:
49:
29:
239:-glucan cellobiohydrolase, cellobiosidase) is an
30:Cellulose 1,4-β-cellobiosidase (non-reducing end)
504:Halliwell G, Griffin M, Vincent R (April 1972).
354:"High level secretion of cellobiohydrolases by
270:-glucan cellobiohydrolase (non-reducing end).
1195:
813:
243:of interest for its capability of converting
8:
346:
344:
342:
455:Eriksson KE, Pettersson B (February 1975).
1202:
1188:
1180:
850:
820:
806:
798:
302:from the non-reducing ends of the chains.
175:
790:at the U.S. National Library of Medicine
635:"Enzymes for Alternative Energy Research"
582:
529:
480:
431:
410:Berghem LE, Pettersson LG (August 1973).
386:
376:
1477:
338:
654:Applied Biochemistry and Biotechnology
26:
604:
602:
313:CBH1 Structure, generated using pymol
7:
416:active on highly ordered cellulose"
482:10.1111/j.1432-1033.1975.tb03921.x
433:10.1111/j.1432-1033.1973.tb02952.x
247:to useful chemicals, particularly
25:
1480:
575:10.1128/JB.180.12.3091-3099.1998
469:European Journal of Biochemistry
420:European Journal of Biochemistry
326:ethanol purity to roughly 99.5%
35:
1084:Alpha-N-acetylgalactosaminidase
709:10.1016/j.biortech.2008.10.057
226:Cellulose 1,4-β-cellobiosidase
1:
1096:Alpha-N-acetylglucosaminidase
41:Cellobiohydrolase monomer,
1519:
459:Sporotrichum pulverulentum
365:Biotechnology for Biofuels
1358:Michaelis–Menten kinetics
666:10.1007/s12010-009-8796-4
174:
34:
1250:Diffusion-limited enzyme
792:Medical Subject Headings
614:Energy Innovation Portal
557:Clostridium thermocellum
356:Saccharomyces cerevisiae
290:-glucosidic linkages in
257:Saccharomyces cerevisiae
1006:Bacterial neuraminidase
756:10.1126/science.1192838
563:Journal of Bacteriology
559:cellobiohydrolase CbhA"
510:The Biochemical Journal
463:Chrysosporium lignorum)
1169:Oxoguanine glycosylase
697:Bioresource Technology
378:10.1186/1754-6834-4-30
322:
314:
1343:Eadie–Hofstee diagram
1276:Allosteric regulation
320:
312:
1353:Lineweaver–Burk plot
1158:N-Glycosyl compounds
1128:Maltase-glucoamylase
1079:Galactosylceramidase
846:Glycoside hydrolases
831:: sugar hydrolases (
1011:Viral neuraminidase
748:2010Sci...330...84G
522:10.1042/bj1270043Pa
1312:Enzyme superfamily
1245:Enzyme promiscuity
1062:Glucosylceramidase
943:Debranching enzyme
867:Sucrase-isomaltase
414:Trichoderma viride
323:
315:
249:cellulosic ethanol
43:Trichoderma reesei
1468:
1467:
1177:
1176:
1148:
1147:
1035:alpha-Mannosidase
909:Alpha-glucosidase
289:
269:
238:
223:
222:
219:
218:
138:metabolic pathway
16:(Redirected from
1510:
1485:
1484:
1476:
1348:Hanes–Woolf plot
1291:Enzyme activator
1286:Enzyme inhibitor
1260:Enzyme catalysis
1204:
1197:
1190:
1181:
1165:DNA glycosylases
931:Beta-glucosidase
851:
822:
815:
808:
799:
776:
775:
727:
721:
720:
692:
686:
685:
649:
643:
642:
631:
625:
624:
622:
620:
606:
597:
596:
586:
550:
544:
543:
533:
501:
495:
494:
484:
452:
446:
445:
435:
407:
401:
400:
390:
380:
362:
348:
287:
267:
236:
176:
39:
27:
21:
1518:
1517:
1513:
1512:
1511:
1509:
1508:
1507:
1493:
1492:
1491:
1479:
1471:
1469:
1464:
1376:Oxidoreductases
1362:
1338:Enzyme kinetics
1326:
1322:List of enzymes
1295:
1264:
1235:Catalytic triad
1213:
1208:
1178:
1173:
1157:
1144:
947:
890:
836:
826:
784:
779:
742:(6000): 84–86.
729:
728:
724:
694:
693:
689:
651:
650:
646:
633:
632:
628:
618:
616:
608:
607:
600:
552:
551:
547:
503:
502:
498:
454:
453:
449:
409:
408:
404:
360:
350:
349:
340:
336:
276:
264:systematic name
45:
23:
22:
15:
12:
11:
5:
1516:
1514:
1506:
1505:
1495:
1494:
1490:
1489:
1466:
1465:
1463:
1462:
1449:
1436:
1423:
1410:
1397:
1384:
1370:
1368:
1364:
1363:
1361:
1360:
1355:
1350:
1345:
1340:
1334:
1332:
1328:
1327:
1325:
1324:
1319:
1314:
1309:
1303:
1301:
1300:Classification
1297:
1296:
1294:
1293:
1288:
1283:
1278:
1272:
1270:
1266:
1265:
1263:
1262:
1257:
1252:
1247:
1242:
1237:
1232:
1227:
1221:
1219:
1215:
1214:
1209:
1207:
1206:
1199:
1192:
1184:
1175:
1174:
1172:
1171:
1161:
1159:
1150:
1149:
1146:
1145:
1143:
1142:
1141:
1140:
1130:
1125:
1120:
1119:
1118:
1113:
1106:Hexosaminidase
1103:
1098:
1093:
1092:
1091:
1081:
1076:
1075:
1074:
1069:
1059:
1054:
1049:
1048:
1047:
1037:
1032:
1031:
1030:
1025:
1018:Galactosidases
1015:
1014:
1013:
1008:
1003:
998:
993:
988:
978:
973:
968:
967:
966:
955:
953:
949:
948:
946:
945:
940:
939:
938:
928:
927:
926:
921:
916:
906:
900:
898:
892:
891:
889:
888:
883:
878:
873:
859:
857:
855:Disaccharidase
848:
838:
837:
827:
825:
824:
817:
810:
802:
796:
795:
783:
782:External links
780:
778:
777:
722:
687:
660:(1–8): 313–7.
644:
626:
598:
569:(12): 3091–9.
545:
496:
447:
402:
337:
335:
332:
275:
272:
221:
220:
217:
216:
211:
205:
204:
199:
193:
192:
187:
181:
180:
172:
171:
160:
153:
152:
147:
141:
140:
135:
129:
128:
123:
117:
116:
111:
105:
104:
99:
93:
92:
87:
81:
80:
76:
75:
70:
64:
63:
58:
52:
51:
47:
46:
40:
32:
31:
24:
14:
13:
10:
9:
6:
4:
3:
2:
1515:
1504:
1501:
1500:
1498:
1488:
1483:
1478:
1474:
1460:
1456:
1455:
1450:
1447:
1443:
1442:
1437:
1434:
1430:
1429:
1424:
1421:
1417:
1416:
1411:
1408:
1404:
1403:
1398:
1395:
1391:
1390:
1385:
1382:
1378:
1377:
1372:
1371:
1369:
1365:
1359:
1356:
1354:
1351:
1349:
1346:
1344:
1341:
1339:
1336:
1335:
1333:
1329:
1323:
1320:
1318:
1317:Enzyme family
1315:
1313:
1310:
1308:
1305:
1304:
1302:
1298:
1292:
1289:
1287:
1284:
1282:
1281:Cooperativity
1279:
1277:
1274:
1273:
1271:
1267:
1261:
1258:
1256:
1253:
1251:
1248:
1246:
1243:
1241:
1240:Oxyanion hole
1238:
1236:
1233:
1231:
1228:
1226:
1223:
1222:
1220:
1216:
1212:
1205:
1200:
1198:
1193:
1191:
1186:
1185:
1182:
1170:
1166:
1163:
1162:
1160:
1156:: Hydrolysing
1155:
1151:
1139:
1136:
1135:
1134:
1131:
1129:
1126:
1124:
1121:
1117:
1114:
1112:
1109:
1108:
1107:
1104:
1102:
1099:
1097:
1094:
1090:
1087:
1086:
1085:
1082:
1080:
1077:
1073:
1072:non-lysosomal
1070:
1068:
1065:
1064:
1063:
1060:
1058:
1055:
1053:
1052:Hyaluronidase
1050:
1046:
1043:
1042:
1041:
1040:Glucuronidase
1038:
1036:
1033:
1029:
1026:
1024:
1021:
1020:
1019:
1016:
1012:
1009:
1007:
1004:
1002:
999:
997:
994:
992:
989:
987:
984:
983:
982:
981:Neuraminidase
979:
977:
974:
972:
969:
965:
964:Alpha-amylase
962:
961:
960:
957:
956:
954:
950:
944:
941:
937:
934:
933:
932:
929:
925:
922:
920:
917:
915:
912:
911:
910:
907:
905:
902:
901:
899:
897:
893:
887:
884:
882:
879:
877:
874:
872:
868:
864:
861:
860:
858:
856:
852:
849:
847:
843:
839:
834:
830:
823:
818:
816:
811:
809:
804:
803:
800:
793:
789:
786:
785:
781:
773:
769:
765:
761:
757:
753:
749:
745:
741:
737:
733:
726:
723:
718:
714:
710:
706:
703:(8): 2411–8.
702:
698:
691:
688:
683:
679:
675:
671:
667:
663:
659:
655:
648:
645:
640:
639:Sigma Aldrich
636:
630:
627:
615:
611:
605:
603:
599:
594:
590:
585:
580:
576:
572:
568:
564:
560:
558:
549:
546:
541:
537:
532:
527:
523:
519:
515:
511:
507:
500:
497:
492:
488:
483:
478:
474:
470:
466:
464:
460:
451:
448:
443:
439:
434:
429:
425:
421:
417:
415:
406:
403:
398:
394:
389:
384:
379:
374:
370:
366:
359:
357:
347:
345:
343:
339:
333:
331:
327:
319:
311:
307:
303:
301:
297:
296:cellotetraose
293:
285:
281:
273:
271:
265:
260:
258:
252:
250:
246:
242:
234:
231:
227:
215:
212:
210:
206:
203:
200:
198:
194:
191:
188:
186:
182:
177:
173:
170:
167:
164:
161:
158:
154:
151:
148:
146:
142:
139:
136:
134:
130:
127:
124:
122:
118:
115:
114:NiceZyme view
112:
110:
106:
103:
100:
98:
94:
91:
88:
86:
82:
77:
74:
71:
69:
65:
62:
59:
57:
53:
48:
44:
38:
33:
28:
19:
1454:Translocases
1451:
1438:
1425:
1412:
1399:
1389:Transferases
1386:
1373:
1230:Binding site
896:Glucosidases
739:
735:
725:
700:
696:
690:
657:
653:
647:
638:
629:
617:. Retrieved
613:
566:
562:
556:
548:
513:
509:
499:
475:(1): 213–8.
472:
468:
462:
458:
450:
426:(1): 21–30.
423:
419:
413:
405:
368:
364:
355:
328:
324:
304:
298:, releasing
278:This enzyme
277:
261:
256:
253:
225:
224:
102:BRENDA entry
42:
18:Exoglucanase
1225:Active site
1123:Iduronidase
1057:Pullulanase
286:of (1→4)-β-
90:IntEnz view
73:37329-65-0
50:Identifiers
1428:Isomerases
1402:Hydrolases
1269:Regulation
1133:Heparanase
1101:Fucosidase
919:Neutral AB
516:(2): 43P.
334:References
300:cellobiose
284:hydrolysis
159:structures
126:KEGG entry
1307:EC number
1067:lysosomal
971:Chitinase
936:cytosolic
924:Neutral C
904:Cellulase
881:Trehalase
871:Invertase
829:Hydrolase
292:cellulose
280:catalyses
245:cellulose
79:Databases
1503:EC 3.2.1
1497:Category
1331:Kinetics
1255:Cofactor
1218:Activity
976:Lysozyme
772:20444539
764:20829451
717:19119005
682:36288505
674:19830597
397:21910902
274:Function
233:3.2.1.91
214:proteins
202:articles
190:articles
163:RCSB PDB
61:3.2.1.91
1487:Biology
1441:Ligases
1211:Enzymes
959:Amylase
886:Lactase
876:Maltase
863:Sucrase
744:Bibcode
736:Science
619:1 March
593:9620957
540:5076675
531:1178673
442:4738092
388:3224389
266:is 4-β-
150:profile
133:MetaCyc
68:CAS no.
1473:Portal
1415:Lyases
1045:Klotho
794:(MeSH)
770:
762:
715:
680:
672:
591:
584:107808
581:
538:
528:
491:235428
489:
440:
395:
385:
371:: 30.
241:enzyme
197:PubMed
179:Search
169:PDBsum
109:ExPASy
97:BRENDA
85:IntEnz
56:EC no.
1367:Types
1154:3.2.2
1138:HPSE2
1023:Alpha
952:Other
842:3.2.1
768:S2CID
678:S2CID
361:(PDF)
145:PRIAM
1459:list
1452:EC7
1446:list
1439:EC6
1433:list
1426:EC5
1420:list
1413:EC4
1407:list
1400:EC3
1394:list
1387:EC2
1381:list
1374:EC1
1116:HEXB
1111:HEXA
1089:NAGA
1028:Beta
1001:NEU4
996:NEU3
991:NEU2
986:NEU1
914:Acid
835:3.2)
760:PMID
713:PMID
670:PMID
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