105:
1004:
491:, which is due to the presence of the four disulfide bridges. It has been suggested also that the difference in the heat stability of the different mabinlin homologues is due to the presence of an arginine residue (heat-stable homologue) or a glutamine (heat-unstable homologue) at position 47 in the B-chain.
479:
With a molecular weight of 10.4kDa, mabinlin-2 is lighter than mabinlin-1. It is a heterodimer consisting of two different chains A and B produced by post-translational cleavage. The A chain is composed of 33 amino acid residues and the B chain is composed of 72 amino acid residues. The B chain
985:
373:
province of China. There are four homologues. Mabinlin-2 was first isolated in 1983 and characterised in 1993, and is the most extensively studied of the four. The other variants of mabinlin-1, -3 and -4 were discovered and characterised in 1994.
541:
During the past decade, attempts have been made to produce mabinlin-2 industrially. The sweet-tasting protein has been successfully synthesised by a stepwise solid-phase method in 1998, however the synthetic protein had an astringent-sweet taste.
923:
618:
Liu X, Maeda S, Hu Z, Aiuchi T, Nakaya K, Kurihara Y (January 1993). "Purification, complete amino acid sequence and structural characterization of the heat-stable sweet protein, mabinlin II".
664:"Structures of heat-stable and unstable homologues of the sweet protein mabinlin. The difference in the heat stability is due to replacement of a single amino acid residue"
552:
tubers, but no explicit results have been reported yet. However, patents to protect production of recombinant mabinlin by cloning and DNA sequencing have been issued.
534:
Mabinlins, as proteins, are readily soluble in water and found to be highly sweet; however, mabinlin-2 with its high heat stability has the best chance to be used as a
934:
596:
Hu Z, He M (1983). "Studies on mabinlin, a sweet protein from the seeds of
Capparis masaikai levl. I. extraction, purification and certain characteristics".
980:, Sun, Samuel S.M.; Xiong, Liwen & Hu, Zhong et al., "Recombinant Sweet protein Mabinlin", issued 2000-04-18, assigned to
817:
Guan RJ, Zheng JM, Hu Z, Wang DC (July 2000). "Crystallization and preliminary X-ray analysis of the thermostable sweet protein mabinlin II".
526:
Mabinlin-3 and -4 sweetness stayed unchanged after 1 hour at 80 °C, while mabinlin-1 loses sweetness after 1 hour at the same condition.
924:"Structures and activities of sweetness-inducing substances (miraculin, curculin, strogin) and the heat-stable sweet protein, mabinlin"
795:
852:
Nirasawa S, Liu X, Nishino T, Kurihara Y (October 1993). "Disulfide bridge structure of the heat-stable sweet protein mabinlin II".
546:
958:
Xiong LW, Sun S (1996). "Molecular cloning and transgenic expression of the sweet protein mabinlin in potato tubers".
1024:
782:
Kohmura M, Ariyoshi Y (October 1998). "Chemical synthesis and characterization of the sweet protein mabinlin II".
887:
Kurihara Y (1992). "Characteristics of antisweet substances, sweet proteins, and sweetness-inducing proteins".
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on molar basis, 10 times sucrose on a weight basis, which make them less sweet than
523:
The sweetness of mabinlin-2 is unchanged after 48 hours incubation at 80 °C.
500:
854:
Biochimica et
Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
336:
259:
182:
81:
459:
EQRGPALRLC CNQLRQVNKP CVCPVLRQAA HQQLYQGQIE GPRQVRRLFR AARNLPNICK IPAVGRCQFT RW
452:
EQRGPALRLC CNQLRQVNKP CVCPVLRQAA HQQLYQGQIE GPRQVRRLFR AARNLPNICK IPAVGRCQFT RW
445:
QPRRPALRQC CNQLRQVDRP CVCPVLRQAA QQVLQRQIIQ GPQQLRRLFD AARNLPNICN IPNIGACPFR AW
438:
EQRGPALRLC CNQLRQVNKP CVCPVLRQAA HQQLYQGQIE GPRQVRQLFR AARNLPNICK IPAVGRCQFT RW
104:
900:
830:
484:
and is connected to the A chain through two intermolecular disulfide bridges.
464:
383:
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225:
148:
47:
662:
Nirasawa S, Nishino T, Katahira M, Uesugi S, Hu Z, Kurihara Y (August 1994).
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10.1002/(SICI)1097-0282(19981005)46:4<215::AID-BIP3>3.0.CO;2-S
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The molecular weights of
Mabinlin-1, Mabinlin-3 and Mabinlin-4 are 12.3
765:
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708:
513:
355:
141:
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Mabinlins sweetness were estimated to be about 100–400 times that of
370:
352:
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Mabinlin-2 is the sweet-tasting protein with the highest known
463:
Amino acid sequence of
Mabinlins homologues are adapted from
520:(3000 times) but elicit a similar sweetness profile.
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494:The sequences of Mabilins cluster with Napins (
889:Critical Reviews in Food Science and Nutrition
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8:
760:Universal protein resource accession number
741:Universal protein resource accession number
722:Universal protein resource accession number
703:Universal protein resource accession number
931:Foods and Food Ingredients Journal of Japan
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609:
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382:The 4 mabinlins are very similar in their
314:
237:
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103:
59:
679:
588:
476:, 12.3 kDa and 11.9 kDa, respectively.
270:
193:
92:
15:
7:
410:QLWRCQRQFL QHQRLRACQR FIHRRAQFGG QPD
417:EPLCRRQFQQ HQHLRACQRY LRRRAQRGGL AD
403:EPLCRRQFQQ HQHLRACQRY IRRRAQRGGL VD
764:for "Sweet protein mabinlin-4" at
745:for "Sweet protein mabinlin-3" at
726:for "Sweet protein mabinlin-2" at
707:for "Sweet protein mabinlin-1" at
681:10.1111/j.1432-1033.1994.tb19077.x
632:10.1111/j.1432-1033.1993.tb19896.x
109:Also known as: Mabinlin II, MAB II
14:
545:Mabinlin-2 has been expressed in
1002:
819:Acta Crystallographica Section D
668:European Journal of Biochemistry
620:European Journal of Biochemistry
922:Kurihara Y, Nirasawa S (1997).
467:biological database of protein.
424:EPLCRRQFQQ HQHLRACQRY LRRRAQRG
1:
933:(174): 67–74. Archived from
866:10.1016/0167-4838(93)90016-K
480:contains two intramolecular
358:extracted from the seed of
1046:
901:10.1080/10408399209527598
831:10.1107/S0907444900005850
313:
236:
159:
102:
58:
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369:), a plant growing in
978:US patent 6051758
391:
1011:at Wikimedia Commons
982:University of Hawaii
508:Sweetness properties
598:Acta Botan. Yunnan.
378:Protein structures
1025:Sugar substitutes
1007:Media related to
365:Capparis masaikai
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825:(Pt 7): 918–9.
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940:on 2013-09-12
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353:sweet-tasting
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942:. Retrieved
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19:
784:Biopolymers
384:amino acids
327:Swiss-model
281:Identifiers
250:Swiss-model
204:Identifiers
173:Swiss-model
115:Identifiers
72:Swiss-model
26:Identifiers
1019:Categories
944:2007-10-01
583:References
547:transgenic
465:Swiss-Prot
323:Structures
318:Search for
297:2SS4_CAPMA
275:Mabinlin 4
246:Structures
241:Search for
220:2SS3_CAPMA
198:Mabinlin 3
169:Structures
164:Search for
131:2SS2_CAPMA
97:Mabinlin 2
68:Structures
63:Search for
42:2SS1_CAPMA
20:Mabinlin 1
966:(2): 147.
577:Thaumatin
536:sweetener
518:thaumatin
501:IPR000617
387:sequences
360:mabinlang
349:Mabinlins
1030:Proteins
1009:Mabinlin
839:10930844
572:Pentadin
567:Monellin
562:Brazzein
556:See also
496:InterPro
356:proteins
337:InterPro
286:Organism
260:InterPro
209:Organism
183:InterPro
120:Organism
82:InterPro
31:Organism
909:1418601
874:8399391
804:9715665
766:UniProt
747:UniProt
728:UniProt
709:UniProt
690:8055976
640:8425538
514:sucrose
498::
430:Chain B
395:Chain A
333:Domains
303:UniProt
256:Domains
226:UniProt
179:Domains
149:UniProt
78:Domains
48:UniProt
987:
907:
872:
837:
802:
762:P80353
743:P80352
724:P30233
705:P80351
688:
638:
550:potato
371:Yunnan
308:P80353
294:Symbol
231:P80352
217:Symbol
154:P30233
128:Symbol
53:P80351
39:Symbol
938:(PDF)
927:(PDF)
367:Levl.
905:PMID
870:PMID
858:1202
835:PMID
800:PMID
686:PMID
636:PMID
456:M-4:
449:M-3:
442:M-2:
435:M-1:
421:M-4:
414:M-3:
407:M-2:
400:M-1:
351:are
142:2DS2
964:111
897:doi
862:doi
827:doi
792:doi
676:doi
672:223
628:doi
624:211
504:).
474:kDa
137:PDB
1021::
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362:(
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34:?
Text is available under the Creative Commons Attribution-ShareAlike License. Additional terms may apply.
