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To cite this article: P.C. Lekshmi , Ranjith Arimboor , K.G. Raghu & A. Nirmala Menon (2012):
Turmerin, the antioxidant protein from turmeric (Curcuma longa) exhibits antihyperglycaemic
effects, Natural Product Research: Formerly Natural Product Letters, 26:17, 1654-1658
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Natural Product Research
Vol. 26, No. 17, September 2012, 1654–1658
SHORT COMMUNICATION
Turmerin, the antioxidant protein from turmeric (Curcuma longa)
Downloaded by [NIIST National Institute for Interdisciplinary Science & Technolgy] at 03:18 23 January 2013
Agroprocessing and Natural Products Division, National Institute for Interdisciplinary Science and
Technology (CSIR), Thiruvananthapuram, Kerala 695019, India
(Received 27 June 2010; final version received 18 April 2011)
1. Introduction
Diabetes, a state of improperly regulated homeostasis of carbohydrate and lipid
metabolism is one of the major killers in recent times. The most prevalent form of
diabetes is non-insulin-dependent diabetes mellitus. Rapid hydrolysis of starch mediated
by pancreatic -amylase and -glucosidases followed by glucose uptake at intestine results
in sudden rise in blood glucose levels, resulting in elevated postprandial hyperglycaemia
(PPH) in type 2 diabetes patients (Gray, 1995). PPH is one of the risk factors inherent to
diabetes, which complicates the treatment (Gin & Rigalleau, 2000). Glucosidase inhibitors
play a major role in managing PPH in diabetic patients (Notkins, 2002). The
conventionally used glucosidase inhibiting drugs such as acarbose and miglitol for the
management of PPH in diabetic patients are known to be associated with a variety of side
effects (Fujisawa, Ikegami, Inoue, Kawabata, & Ogihara, 2005). In this context, the search
for glucosidase inhibitors from natural sources with lesser side effects attracts more
researchers’ interests.
In Indian traditional medicine ‘Ayurveda’, turmeric (Curcuma longa) rhizomes
have been given a major importance in the treatment of diabetes and related disorders.
A wide spectrum of physiological effects has been attributed to its rhizome both in
traditional and modern medicinal systems. Curcuminoids and turmerin were reported to
be the major bioactive constituents of the rhizome. Curcuminoids are reported to inhibit
-amylase activity (Du et al., 2006). Turmerin, a water-soluble protein with a molecular
weight of 34 kDa (Smitha, Dhananjaya, Dinesha, & Srinivas, 2009), has been shown to be
an antioxidant (AO) protein (Srinivas, Shalini, & Shylaja, 1992). Its ability to protect
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Figure 1. Dose dependent inhibition of -amylase and -glucosidase shown by the turmerin-
enriched extract (Mean SD, n ¼ 3).
Figure 2. DPPH, superoxide and ABTS radical scavenging and Fe(II) chelation capacity of
turmerin-enriched extract (Mean SD, n ¼ 3).
Natural Product Research 1657
48 mg mL1) was lower ( p50.05) than that of catechin (IC50 ¼ 16 mg mL1). IC50 values
obtained for Fe(II) chelation by turmerin and EDTA were 101 and 6 mg mL1,
respectively. A moderate AO potential of turmerin was demonstrated by these in vitro
assays. Though a number of AO compounds have been isolated and characterised from
dietary sources as effective radical scavengers, very few reports are available on plant
proteins showing AO activity. Smitha et al. (2009) reported hydroxyl radical scavenging
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and lipid peroxidation inhibitory capacities of turmerin. DPPH, ABTS and superoxide
radical-scavenging and chelation capacities of turmerin demonstrated in this study further
confirmed the AO nature of turmerin.
3. Conclusions
The turmeric protein, turmerin-enriched extract showed considerable glucosidase inhibi-
tion potential along with moderate AO capacity. Since diabetes and related disorders are
largely associated with increased oxidative stress, therapeutic agents with both antidiabetic
and AO efficacies gain special interest. Water solubility and non-toxic nature of turmerin
might further enhance its potential as an antidiabetic agent. The high -amylase and
-glucosidase inhibitory potentials of turmerin evidenced by this study along with the
reports on the inhibitory potential of curcuminoids could rationalise the traditional usage
of turmeric as an antidiabetic agent. Further in vivo studies are warranted to fully elucidate
the antidiabetic potential of turmerin.
Supplementary material
Experimental details relating to this article are available online.
Acknowledgements
We gratefully acknowledge the financial support provided by Council for Scientific and Industrial
Research, India.
References
Chethankumar, M. (2010). Turmerin, a protein from Curcuma longa L. prevent oxidative organ damage against
Naja naja venom phospholipase A2 in experimental animal. Journal of Current Pharmaceutical Research,
3, 29–34.
Cohly, H.H.P., Hammet, C., Angel, M.F., Kanji, V., Taylor, V., Benghuzzi, H., & Markov, A.K. (2002). Effect
of turmerin on endothelial denudation by air drying. International Journal of Molecular Sciences, 3,
985–991.
Dayler, C.S.A., Mendesa, P.A.M., Pratesa, M.V., Bloch Jr, C., Francob, O.L., & Grossi-de-Sáab, M.F. (2005).
Identification of a novel bean -amylase inhibitor with chitinolytic activity. FEBS Letters, 579,
5616–5620.
Du, Z., Liu, R., Shao, W., Mao, X., Ma, L., Gu, L., . . . , Chan, A.S.C. (2006). -Glucosidase inhibition of natural
curcuminoids and curcumin analogs. European Journal of Medicinal Chemistry, 41, 213–218.
Fujisawa, T., Ikegami, H., Inoue, K., Kawabata, Y., & Ogihara, T. (2005). Effect of two alpha-glucosidase
inhibitors, voglibose and acarbose, on postprandial hyperglycaemia correlates with subjective abdominal
symptoms. Metabolism, 54, 387–390.
Gin, H., & Rigalleau, V. (2000). Post-prandial hyperglycaemia and Diabetes. Diabetics and Metabolism, 26,
265–272.
Gray, D.M. (1995). Carbohydrate digestion and absorption-role of small intestine. New England Journal of
Medicine, 29, 1225–1230.
Greismacher, A., Kindhauser, M., Andert, S.E., Andert, M.E., Schreiner, W., Toma, C., . . . , Mueller, M.D.
(1995). Enhanced serum levels of thiobarbituric-acid-reactive substances in diabetes mellitus. American
Journal of Medicine, 98, 469–474.
Hirsh, A.J., Yao, S.Y., Young, J.D., & Cheeseman, C.I. (1997). Inhibition of glucose absorption in the rat
jejunum: A novel action of alpha-D-glucosidase inhibitors. Gastroenterology, 113, 205–211.
1658 P.C. Lekshmi et al.
Kumar, S., Singh, N., Sinha, M., Dube, D., Singh, S.B, Bhushan, A., . . . , Singh, T.P. (2010). Crystal structure
determination and inhibition studies of a novel xylanase and a-amylase inhibitor protein (XAIP) from
Scadoxus multiflorus. FEBS Journal, 277, 2868–2882.
Mclauchlan, W.R., Garcia-conesa, M.T., Williamson, G., Roza, M., Ravestein, P., & Maat, J. (1999). A novel
class of protein from wheat which inhibits xylanases. Biochemistry Journal, 338, 441–446.
Notkins, A.L. (2002). Immunologic and genetic factors in type 1 diabetes. Journal of Biological Chemistry, 277,
4354–4358.
Downloaded by [NIIST National Institute for Interdisciplinary Science & Technolgy] at 03:18 23 January 2013
Smitha, S., Dhananjaya, B.L., Dinesha, R., & Srinivas, L. (2009). Purification and characterisation of a 34 kDa
antioxidant protein (-turmerin) from turmeric (Curcuma longa) waste grits. Biochimie, 91, 1156–1162.
Srinivas, L., Shalini, V.K., & Shylaja, M. (1992). Turmerin: A water soluble antioxidant peptide from turmeric
(Curcuma longa). Archives of Biochemistry and Biophysics, 292, 617–623.
Tiengburanatam, N., Boonmee, N., Sangvanich, P., & Karnchanatat, A. (2010). A novel -glucosidase inhibitor
protein from the rhizomes of Zingiber ottensii Valeton. Applied Biochemistry and Biotechnology, 162,
1938–1951.