38:
728:
281:, weighing 12.5 kDa (curculin 1) and 12.7 kDa (curculin 2), respectively. While each of the two isoforms is capable of forming a homodimer, these do not possess the sweet taste nor the taste-modifying activity of the heterodimeric form. To avoid confusion, the heterodimeric form is sometimes referred to as "neoculin".
373:
membranes while a second active site fits into the sweet receptor site. The latter site is thought to be responsible for the induction of sweetness. Presence of Ca and/or Mg, water and acids tune the binding of the active site of curculin to the receptor site and therefore modify perceived sweetness.
365:
The taste-modifying activity of curculin is reduced in the presence of ions with two positive charges (such as Ca and Mg) in neutral pH solutions, although these ions have no effect in acidic solutions. In the same way, monovalent ions (such as Na and Cl) have no effect in solutions with either
386:
Like most proteins, curculin is susceptible to heat. At a temperature of 50 °C (122 °F) the protein starts to degrade and lose its "sweet-tasting" and "taste-modifying" properties, so it is not a good candidate for use in hot or processed foods. However, below this temperature both
415:
In addition to challenges related to commercial production of the protein, there are many regulatory and legal issues remaining to be resolved before it can be marketed as a sweetener. Curculin currently has no legal status in
277:
The active form of curculin is a heterodimer consisting of two monomeric units connected through two disulfide bridges. The mature monomers each consist of a sequence of 114
343:
curculin-1 and curculin-2 adapted from Swiss-Prot biological database of protein sequences. Intra-chain disulfide bonds in bold, inter-chain disulfide bonds underlined.
708:
Kurihara Y, Nirasawa S (1997). "Structures and activities of sweetness-inducing substances (miraculin, curculin, strogin) and the heat-stable sweet protein, mabinlin".
408:, but the recombinant protein did not exhibit "sweet-tasting" or "taste-modifying" activity. However, a 2004 study obtained a recombinant curculin, expressed in
673:
Koizumi A, Nakajima K, Asakura T, et al. (29 June 2007). "Taste-modifying sweet protein, neoculin, is received at human T1R3 amino terminal domain".
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Suzuki M, Kurimoto E, Nirasawa S, et al. (August 2004). "Recombinant curculin heterodimer exhibits taste-modifying and sweet-tasting activities".
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Curculin is considered to be a high-intensity sweetener, with a reported relative sweetness of 430-2070 times sweeter than sucrose on a weight basis.
269:
activity; however, unlike miraculin, it also exhibits a sweet taste by itself. After consumption of curculin, water and sour solutions taste sweet.
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71:
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Yamashita H, Akabane T, Kurihara Y (April 1995). "Activity and stability of a new sweet protein with taste-modifying action, curculin".
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properties of curculin are unaffected in basic and acidic solutions, so it has potential for use in fresh foods and as a table-top
432:, according to the List of Existing Food Additives established by the Ministry of Health and Welfare (English publication by
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Although the "sweet-inducing" mechanism is unknown, it is believed that one active site of curculin strongly binds to the
758:
489:"Purification and complete amino acid sequence of a new type of sweet protein taste-modifying activity, curculin"
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596:
Kurihara Y (1992). "Characteristics of antisweet substances, sweet proteins, and sweetness-inducing proteins".
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solution, was observed after holding curculin in the mouth in combination with clear water or acidified water (
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362:), respectively. The sweet taste lasts for 5 minutes with water and 10 minutes with an acidic solution.
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Because curculin is not widely found in nature, efforts are underway to produce a
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Curculin appears to use a unique binding site at the amino terminal of
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Yamashita H, Theerasilp S, Aiuchi T, et al. (September 1990).
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412:, exhibiting "taste-modifying" and "sweet-tasting" properties.
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that was discovered and isolated in 1990 from the fruit of
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form of the protein. In 1997, curculin was expressed in
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577:Universal protein resource accession number
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710:Foods and Food Ingredients Journal of Japan
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354:A sweet taste, equivalent to a 6.8% or 12%
25:Sweet protein with taste-modifying activity
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310:2, 1-50: DSVLLSGQTL YAGHSLTSGS YTLTIQNN
285:1, 1-50: DNVLLSGQTL HADHSLQAGA YTLTIQNK
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493:The Journal of Biological Chemistry
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1:
545:10.1016/j.febslet.2004.07.073
506:10.1016/S0021-9258(18)55464-8
424:. However it is approved in
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687:10.1016/j.bbrc.2007.04.171
321:RLTLRSDG NLIIYDDNNM VVWGSD
296:RLTLLSDG NLVIYDHNNN DVWGSA
17:
610:10.1080/10408399209527598
325:WGN NGTYALVLQQ DGLFVIYGPV
300:WGD NGKYALVLQK DGRFVIYGPV
205:
112:
35:
18:Not to be confused with
652:10.1093/chemse/20.2.239
314:N LVKYQHGRQI WASDTDGQGS
289:N LVKYQNGRQI WASNTDRRGS
366:neutral or acidic pH.
735:at Wikimedia Commons
581:for "Curculin-2" at
570:for "Curculin-1" at
347:Sweetness properties
328:2, 101-113: LWPLGLNG
303:1, 101-114: LWSLGPNG
265:, curculin exhibits
254:Curculigo latifolia
166:Molineria latifolia
73:Molineria latifolia
339:sequence of sweet
759:Sugar substitutes
731:Media related to
273:Protein structure
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721:External links
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539:(1–3): 135–8.
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382:As a sweetener
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259:Hypoxidaceae
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396:recombinant
360:citric acid
279:amino acids
247:is a sweet
219:Swiss-model
177:CURC2_CURLA
155:Identifiers
126:Swiss-model
62:Identifiers
42:A curculin
743:Categories
467:References
337:Amino acid
215:Structures
210:Search for
150:Curculin-2
122:Structures
117:Search for
84:CURC_CURLA
31:Curculin-1
764:Curculigo
461:Thaumatin
451:Miraculin
389:sweetener
263:miraculin
44:homodimer
733:Curculin
712:: 67–74.
695:17499612
553:15327988
456:Monellin
446:Brazzein
440:See also
430:additive
341:proteins
261:). Like
245:neoculin
241:Curculin
229:InterPro
160:Organism
136:InterPro
67:Organism
56:.
20:Curcumin
660:7583017
618:1418601
583:UniProt
572:UniProt
515:2394746
410:E. coli
401:E. coli
356:sucrose
249:protein
225:Domains
195:UniProt
132:Domains
102:UniProt
46:. From
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658:
616:
579:Q6F495
568:P19667
551:
513:
376:TAS1R3
307:R RVNG
200:Q6F495
174:Symbol
107:P19667
81:Symbol
434:JETRO
426:Japan
406:yeast
332:R SLN
691:PMID
656:PMID
614:PMID
549:PMID
511:PMID
420:and
404:and
188:2D04
95:2DPF
53:2DPF
683:doi
679:358
648:doi
606:doi
541:doi
537:573
501:doi
497:265
436:).
243:or
183:PDB
90:PDB
49:PDB
745::
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330:C
323:C
319:C
312:C
305:C
298:C
294:C
287:C
257:(
22:.
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