SAJB-01948; No of Pages 6

South African Journal of Botany xxx (2017) xxx–xxx

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South African Journal of Botany

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Mangiferin from Mangifera indica fruits reduces post-prandial glucose

level by inhibiting α-glucosidase and α-amylase activity
V. Sekar, S. Chakraborty, S. Mani, V.K. Sali, H.R. Vasanthi ⁎
Natural Products Research Laboratory, Department of Biotechnology, Pondicherry University, Puducherry 605014, India

a r t i c l e i n f o a b s t r a c t

Article history: Background: Mangiferin, is a xanthone glycoside mainly present in Mangifera indica fruits and few other
Received 20 November 2017 medicinal plants that are cultivated in the tropical and sub-tropical regions. Mangiferin has a wide spectrum of
Received in revised form 17 January 2018 biomedical properties from anti-microbial to anti-cancer activities.
Accepted 1 February 2018 Aim: In the present study, the mangiferin content in the methanolic extract of unripe and ripe mango pulp
Available online xxxx
was compared and quantified by Reverse Phase HPLC method. Further, inhibitory action of mangiferin on α-
Edited by Kannan Ragupathi Raja Rengasamy
glucosidase and α-amylase enzymes which play a vital role in the regulation of serum glucose level was studied.
Materials and methods: The enzyme inhibitory nature of mangiferin was tested using in silico docking analysis
Keywords: with Autodock software and was further confirmed by in vitro α-glucosidase and α-amylase biochemical assays.
Mangiferin Results: The results of this study reveal that, mangiferin content was higher in ripe methanolic extract than in
RP HPLC unripe. Further, mangiferin exhibited better enzyme inhibitory action in silico with α-glucosidase with a binding
α-Glucosidase energy of −7.4 kcal/mol than α-amylase. This was concurred with α-glucosidase in vitro assays wherein the IC50
α-Amylase of mangiferin was 36.84 μg/ml and that of ripe mango extract was 112.8 μg/ml when compared to the standard
Mangifera indica acarbose 21.33 μg/ml.
Conclusion: Evidently, it can be concluded that mangiferin from Mangifera indica fruits slows down the glucose
metabolism and thereby could be used as a possible hypoglycemic agent owing to its enzyme inhibitory
properties.
© 2017 SAAB. Published by Elsevier B.V. All rights reserved.

1. Introduction affects the pathophysiology and ensures complications like nephropa-

The recent statistics on the steady increase in the number of
diabetics across the world poses a major challenge for biomedical
researchers and health care professionals. Diabetes mellitus (DM) is a
metabolic disorder characterized by chronic hyperglycemia due to
abnormality in insulin secretion or insulin receptor or defects in metab-
olism of carbohydrates in association with liver or kidney or pancreatic
damage. In addition to these factors, DM can also be very much influ-
enced by genetic susceptibility, sedentary and other harmful lifestyle
practices such as alcoholism, smoking, etc. (Marx, 2002). The persistent
factor which propels DM as a challenging disease is the elevated blood
glucose level or hyperglycemia. Chronic hyperglycemia, besides being
deleterious to the metabolism, on a cellular level reacts with structural
or plasma proteins – glycation reaction which results in advanced
glycated end products (AGE). The AGEs modulates the structural
integrity, stability and function of the proteins and thereby promptly
⁎ Corresponding author at: Department of Biotechnology, School of Life Sciences,
Pondicherry University, Puducherry 605014, India.
E-mail addresses: hannah.dbt@pondiuni.edu.in, hrvasanthi@gmail.com
(H.R. Vasanthi).
thy, retinopathy or neuropathy (Brownlee, 2001; Goh and Cooper,
2008).
The therapeutic strategies for managing diabetes encompasses a
range of drugs, including biguanides, prescribed as first line of medica-
tion, to decrease glucose production in the liver. Also, the sulfonylureas
stimulates the pancreatic β cells for insulin release (Gupta et al., 2016)
One such therapeutic option to subside the post-prandial hyperglyce-
mia is the enzyme inhibitors and acarbose is the most commonly
used enzyme inhibitor (Obih et al., 2016). Alpha-glucosidase and
α-amylase are the two enzymes responsible for the hydrolysis of
long chain complex carbohydrates into simple chain glucose molecules
to facilitate their transport inside the cells. Acarbose acts as an inhibitor
to these enzymes, hence ensures the delay in the increase of post
prandial hyperglycemic state after a meal (Baron, 1998; Chiasson
et al., 2002). Although, acarbose is a promising therapeutic option for
diabetics, but in the long run, like any other therapeutic drug it does
have a few setbacks that cannot be overlooked. Continous intake of
acarbose are proven to exhibit side effects like stomach distention,
flatulence, diarrhoea, etc. (Chiasson et al., 2002).
It is not an entirely a new concept of phytochemical intervention
when modern therapeutics takes a step down in its full potential to
treat a disease, as phytomedicines have been used extensively for

https://doi.org/10.1016/j.sajb.2018.02.001
0254-6299/© 2017 SAAB. Published by Elsevier B.V. All rights reserved.

Please cite this article as: Sekar, V., et al., Mangiferin from Mangifera indica fruits reduces post-prandial glucose level by inhibiting α-glucosidase
and α-amylase activity, South African Journal of Botany (2017), https://doi.org/10.1016/j.sajb.2018.02.001
2 V. Sekar et al. / South African Journal of Botany xxx (2017) xxx–xxx
metabolism related disorders since time immemorial. Several medicinal
plants such as Tinospora cordifolia (Sangeetha et al., 2011), Salacia
reticulata (Li et al., 2008; Im et al., 2009) and many other Indian medic-
inal plants (Grover et al., 2002) are being used to treat diabetes and its
complications. Mangifera indica known for its drupe fruit is also
known for its anti-diabetic potential (Wauthoz et al., 2007).
It is interesting to note that mangiferin, a polyphenol present in
many medicinal plants which exhibits hypoglycemic potential is also
present in mangoes. Herein, we have evaluated the level of mangiferin
in both ripe and unripe Mangifera indica fruits and their potential as
enzyme inhibitors of α-glucosidase and α-amylase using in silico and
in vitro assays.
2. Materials and methods
2.1. Chemicals
Alpha-amylase from Aspergillus oryzae and mangiferin were pur-
chased from Sigma Aldrich, USA. Alpha-glucosidase from Saccharomyces
cervesiae and HPLC grade solvents were purchased from SRL Chemicals,
Mumbai, India. Acarbose was purchased from Santa Cruz Biotechnology,
USA. All other solvents and chemicals used were of analytical grade.
2.2. Preparation of plant extracts
Fresh unripe and ripe Totapuri mangoes were procured from a near-
by organic farm in Puducherry. The pulp of ripe and unripe mangoes
were removed manually and crushed. The pulp was subjected to
Soxhlet extraction using 95% methanol for 6–8 h. The extract was con-
centrated using a rotary evaporator under reduced pressure
(Sellamuthu et al., 2009). This extract was used for further analysis.
2.3. Quantification of mangiferin by HPLC
Reverse Phase High Performance Liquid Chromatography (RP-HPLC)
was performed to check and quantify the mangiferin content in both the
ripe and unripe pulp extracts. C18-250X4.60 mm 5 μm, 100 Å column
was used to separate mangiferin. The mobile phase consisting of
HPLC grade water with potassium phosphate monobasic and ortho-
phosphoric acid and the stationary phase was acetonitrile was used
for the analysis. A flow rate of 0.5 ml/min was maintained and the
UV–visible detector wavelength was set at 254 nm (Geodakyan et al.,
1992).
2.4. In silico docking analysis
Molecular docking of mangiferin with the two enzymes α-amylase
and α-glucosidase was done to identify the binding of the protein
with the ligand. Hence, the details of α-glucosidase (PDB ID 5NN4.A)
and α-amylase (PDB ID 4X9Y) were retrieved from the Protein Data
Bank (PDB) (www.pdb.org/pdb). Using Pymol, the structures of the
receptors were prepared for docking by removing the co-crystallized
ligand and additional water molecules to make it as a nascent receptor.
Ligand structures were generated by Chemsketch (www.acdlabs.com)
in mol format and the generated structures were converted into
PDB format using Chimera (http://www.cgl.ucsf.edu/chimera). Subse-
quently, the generated PDB structures were used for docking by using
flexible docking protocol (Trott and Olson, 2010), Auto dock (Auto
dock tools- 1.5.4 version).
2.5. Enzyme inhibitory assays
2.5.1. Alpha glucosidase assay
Alpha-glucosidase inhibitory assay is based on the influence of
α-glucosidase for the breakdown of maltose to glucose and was
performed with few modifications (Li et al., 2004). Briefly, 0.6 U/ml of
Please cite this article as: Sekar, V., et al., Mangiferin from Mangifera indica fruits reduces post-prandial glucose level by inhibiting α-glucosidase
and α-amylase activity, South African Journal of Botany (2017), https://doi.org/10.1016/j.sajb.2018.02.001
enzyme solution was pre-incubated with the test sample and standard
drug for 5 min. The reaction was initiated by adding 370 mM of sucrose,
after incubation at 37 °C for 30 min and terminated by heating at
90–100 °C. The glucose is measured by GOD-POD method at
546 nm using a semi auto-analyser. The enzyme activity is directly pro-
portional to the liberated glucose. Acarbose was used as a positive
control.
2.5.2. Alpha amylase assay
The α-amylase assay was performed by protocol of (Kusano et al.,
2010) with slight modifications. Substrate was prepared by dissolving
200 mg starch in 25 ml of sodium hydroxide (0.4 M) by heating at
100 °C for 5 min. After cooling, pH was adjusted to 7.0 and the final
volume was made up to 100 ml using distilled water. Acarbose was
used as a positive control. Forty microliter of substrate solution was
pre-incubated at 37 °C for 3 min with 20 μl of acarbose and test material
at varying concentrations, followed by 20 μl of 3 U/ml α-amylase
(20 mM phosphate buffer with 6.7 mM Nacl, pH 6.9) and incubated at
37 °C for 15 min. Termination of the reaction was carried out by adding
80 μl of HCl (0.1 M), followed by addition of 100 μl of iodine reagent
(2.5 mM). The absorbance was measured at 630 nm.
2.6. Statistical analysis
All the data were expressed as mean ± SEM of triplicates. IC50 values
were determined from dose-inhibition (curve fit) using non-linear re-
gression in Graph Pad Prism Software, version 5 (Graph Pad Software,
San Diego, CA, USA).
3. Results and discussion
Dietary recommendations to cure and prevent DM include fresh
vegetables and fruits. Misconception, moderate awareness and
inadequate research in functional foods have led the growing popula-
tion to approach for synthetic therapy in the developing countries
(Lock et al., 2005). Owing to the advancement of ripening in fruits,
they contain low starch, high sugars, polyphenols, flavonoids etc.
(Moneruzzaman et al., 2008). In the present study in order to identify
if mangoes can be considered as functional food, the quantity of
mangiferin, the principle bioactive compound, was measured in
ripe as well as unripe mangoes and identified its α-glucosidase and
α-amylase inhibiting potential to act as an agent against post-prandial
hyperglycemia.
3.1. Quantification of mangiferin in mango pulp
Mangiferin is a C-glycosyl xanthone, chemically known as C2-β-D-
glucopyranosyl- 1,3,6,7-tetrahydroxyxanthone (Fig. 1) and Mangifera
indica is the primary and easily available source of mangiferin. The
content of the same is found in different parts of the tree which includes
the leaves, fruits, seed kernels, peels, heartwood, and stem bark and the
Fig. 1. Chemical structure of Mangiferin.
 V. Sekar et al. / South African Journal of Botany xxx (2017) xxx–xxx 3

latter contains the highest mangiferin content comparatively (Barreto anti-diabetic agent, the mangiferin content in the ripe and unripe pulp
et al., 2008). methanolic extracts were checked and quantified. The chromatograms
As this study was mainly focused on the mangiferin present in the are shown in (Fig. 2) and the estimated amount based on the retention
pulps of ripe and unripe Mangifera indica fruits to consider it as an time and peak area are given in Table 1). Identification and comparison

A)

B)

C)

Fig. 2. HPLC Chromatogram. Representative HPLC profile A) standard mangiferin B) methanloic extract of unripe mango pulp (* mangiferin peak) C) methanolic extract of ripe mango pulp
(* mangiferin peak).

Please cite this article as: Sekar, V., et al., Mangiferin from Mangifera indica fruits reduces post-prandial glucose level by inhibiting α-glucosidase
and α-amylase activity, South African Journal of Botany (2017), https://doi.org/10.1016/j.sajb.2018.02.001
4 V. Sekar et al. / South African Journal of Botany xxx (2017) xxx–xxx

Table 1 its chemical structure obeys the Lipinski's rule of five (Lipinski et al.,
Quantification of mangiferin based on the HPLC chromatogram. 1997) and is vividly discussed (Saha et al., 2016). However, there are
Sample Retention time Area Quantity major concerns on the bioavailability of mangiferin both in vivo and
Mangiferin 7.237 30143678 100 μg/ml
in vitro. For instance, better than the pure mangiferin, mangiferin com-
Unripe mango pulp 7.639 24746181 1.32 μg/g plexed with phospholipids have better bioavailability in rats (Ma et al.,
Ripe mango pulp 7.127 363836699 3.06 μg/g 2014). Similarly, mangiferin with soya phospholipid complex was prov-
en to have 9.75 fold increase in the bioavailability in vivo (Bhattacharyya
et al., 2014). A study on the pharmacokinetics of mangiferin and its me-
of mangiferin present in the extracts were correlated with the chro- tabolite in rodent model by administration of Rhizoma Anemarrhenae
matogram of standard mangiferin (Fig. 2A). Based on the retention decoction yet again revealed that mangiferin's bioavailabilty could be
time and peak area, the concentration of mangiferin from ripe mango vastly improved by complex interactions with other compounds (Tian
pulp extract was 3.06 μg/g while in unripe mango pulp extract was et al., 2016). In addition, to the mangiferin complexes, researchers
1.32 μg/g. The exact reason why mangiferin content was higher in ripe have developed derivatives of parent mangiferin to improve the phar-
mango pulp extract than in unripe mango pulp extract remains to be macological activities. Esterified derivatives of mangiferin were studied
unclear as the biological synthesis of mangiferin is a multi-step process and identified to show improved hypoglycemic and lipid solubility
(Ehianeta et al., 2016). Mangiferin embodies as an orally active drug as properties (Xue-Jian et al., 2013). Earlier study on the inhibitory activity

A) B)

C) D)

Fig. 3. Docking analysis. In silico docking analysis A) mangiferin with α-glucosidase B) mangiferin with α-amylase C) acarbose with α-glucosidase D) acarbose with α-amylase.

Please cite this article as: Sekar, V., et al., Mangiferin from Mangifera indica fruits reduces post-prandial glucose level by inhibiting α-glucosidase
and α-amylase activity, South African Journal of Botany (2017), https://doi.org/10.1016/j.sajb.2018.02.001
 V. Sekar et al. / South African Journal of Botany xxx (2017) xxx–xxx
Table 2
Binding energy and active site amino acids on docking mangiferin with respective proteins.
S.No. Ligand-protein Binding energy (kcal/mol)
1. Mangiferin Vs α-Glucosidase −7.4
2. Mangiferin Vs α-Amylase −5.67
3 Acarbose Vs α-Glucosidase −7.3
4 Acarbose Vs α-Amylase −7.1
against protein tyrosine phosphatase 1B (PTP1B), to study the anti-dia-
betic and obesity activity of benzyl derivatives of mangiferin revealed
better activity than the mangiferin molecule (Hu et al., 2007). These
studies on the derivatives provide better insight on the specific pharma-
cological actions and better understanding on the structure–activity re-
lationships. The bioavailability and liposolubility concern of mangiferin
in the mammalian system has to be evaluated to consider the ripe
Mangifera indica fruits as an anti-diabetic agent.
3.2. Enzyme inhibitory activity by in silico analysis
Alpha-glucosidase and α-amylase are two key enzymes in
dietary carbohydrate metabolism. Alpha-amylase (1,4-α-D-glucan-
glucanohydrolase) is a starch metabolizing enzyme which hydrolyses
the polysaccharides to glucose and maltose oligosaccharides
(Koukiekolo et al., 2001). These hydrolysed oligosaccharides are then
acted upon by α-glucosidase which is a membrane bound enzyme
present in the epithelium of brush borders in the small intestines. This
enzyme hydrolyses at the non-reducing links to release the bound
alpha-glucose and thus increasing the glucose level in the serum
(Kimura, 2000). For the effective management of DM, inhibiting the
enzymes responsible for carbohydrate digestion ensures delay in the in-
crease of post prandial glucose in the serum (Bischoff, 1995). As long
term consumption of acarbose leads to certain complications in the di-
gestive system, medicinal plant extracts and their bioactive components
are evaluated for enzyme inhibitory properties (Tundis et al., 2010). In
this study, mangiferin molecule was docked with the protein ligands
α-glucosidase and α-amylase. With α-glucosidase, mangiferin was
docked in the catalytic site and interacted with amino acids with a
binding energy of −7.4 kcal/mol showing positive binding and poten-
tial inhibition (Fig. 3A, Table 2). In the case of α-amylase, mangiferin
was bound with a binding energy of −5.67 kcal/mol showing positive
binding and potential inhibition (Fig. 3B, Table 2). When the docking
interaction of mangiferin with both the enzymes were compared, the
results reveal mangiferin showed better α-glucosidase inhibition than
α-amylase as the former had higher intermolecular energy. These
interactions of mangiferin with α-glucosidase and α-amylase were
compared with the interaction of acarbose with α-glucosidase
and α-amylase whose binding energies were − 7.3 kcal/mol and
− 7.1 kcal/mol, respectively. It is evident that, mangiferin's enzyme
inhibitory energy is comparable to acarbose. Docking analysis results
prompted us to further explore the enzyme inhibitory activity via
biochemical assays.
3.3. Enzyme inhibitory activity by in vitro assays
To establish a relationship between enzyme inhibiting activity of
mangiferin and the methanolic extracts of ripe and unripe mango
pulp, α-glucosidase and α-amylase inhibitory assays were performed
with all three samples and acarbose was used as a positive control.
Table 3
Inhibitory concentration of extracts, mangiferin and standard drug acarbose.
IC50 (μg) Acarbose Mangiferin Mango (Ripe) Mango (Unripe)
α- amylase 11.18 μg/ml 63.57 μg/ml 287.6 μg/ml 318.1 μg/ml
α- glucosidase 21.33 μg/ml 36.84 μg/ml 112.8 μg/ml 127.0 μg/ml
Please cite this article as: Sekar, V., et al., Mangiferin from Mangifera indica fruits reduces post-prandial glucose level by inhibiting α-glucosidase
and α-amylase activity, South African Journal of Botany (2017), https://doi.org/10.1016/j.sajb.2018.02.001
5
Amino acids
Asp-1157, Asp-1279, Arg-1510,Lys-1460 and His-1584
`Asp-195, Asp-197, Glu-233, Glu-240 and Asp-300
Arg- 608, Tyr- 360, His- 717
Ser- 19, Asn-20, Arg-413, Gly-349
The IC50 values of each sample corresponding to the assays are tabulated
in (Table 3). As expected, mangiferin showed better enzyme inhibitory
activity with IC50 of α-glucosidase 36.84 μg/ml and that of α-amylase is
63.57 μg/ml. Ripe mango extracts exhibited high enzyme inhibitory
potential against α-glucosidase with an IC50 112.8 μg/ml and that of
α-amylase is 287.6 μg/ml. The unripe mango pulp extract exhibited an
enzyme inhibition of α-glucosidase corresponding to 127.0 μg/ml and
that of α-amylase as 318.1 μg/ml. It is interesting to note that, several
in vitro and in silico studies have been carried out in mangiferin from
various sources (Picot et al., 2017). However, our team mainly focused
on mangiferin, from ripe and unripe Mangifera indica fruit pulps, to
justify the claim that they serve as an anti-diabetic functional food.
To aid in food selection for diabetic population, the Glycemic Index
(GI) is formulated. GI is the post-prandial increase in blood glucose
after the consumption of a food item, with pure glucose as reference,
GI of foods can be classified as, low (0–55), medium (55–69) and high
(≥70) (Jenkins et al., 2002). Based on our study, the mangiferin content
and enzyme inhibitory activity was more pronounced in the ripe mango
methanolic extract. Mangoes fall under the low GI category which cor-
responds to the GI value of 51 (Atkinson et al., 2008). Thus from the
above facts it can be inferred that ripe mangoes with more mangiferin
content can be considered as a potential functional food for diabetics.
However, further in vivo studies are warranted to check the influence
of mangiferin and Mangifera indica fruits in the proteomic level.
4. Conclusion
In this study, mangiferin, a phytocompound with various biomedical
properties was quantified in unripe and ripe Mangifera indica fruit pulp
methanolic extracts and it was found that the ripe extract had a slightly
higher concentration of mangiferin than the unripe extract. The enzyme
inhibitory nature of mangiferin was evaluated both by in silico and
in vitro approach employing docking analysis and enzymatic assays
and the results revealed that mangiferin showed better alpha-
glucosidase inhibitory activity. Based on the results, it can be concluded
that the enzyme inhibitory nature of mangiferin could be an added
reason to further explore mangiferin's influence on the metabolism in
a genomic and proteomic level.
Conflict of interest
The authors declare that there are no conflicts of interest.
Acknowledgement
The authors would like to express their gratitude to UGC (SAP) and
DST (FIST) grants for infrastructural facilities in the Department of
Biotechnology, Pondicherry University to execute the present work.
We are also grateful for the Pondicherry University Fellowship to VS
from UGC, DBT fellowship to SC, DST fellowship to SM and RGNF
fellowship from UGC to VKS.
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