Rev. Colomb. Cienc. Quím. Farm., Vol.44(1), 72-89, 2015 www.farmacia.unal.edu.co Artículo de investigación científica Inhibitory effects of an extract of fruits of Physalis peruviana on some intestinal carbohydrases Diana Patricia Rey1, Luis Fernando Ospina2, Diana Marcela Aragón2,3* 1 Corporación Tecnológica de Bogotá, Bogotá, D. C., Colombia. 2 Grupo de Investigación Principios Bioactivos en Plantas Medicinales, Departamento de Farmacia, Facultad de Ciencias, Universidad Nacional de Colombia, Cra. 30 No. 45-03, Bogotá, D. C., Colombia. 3 Grupo de Investigación en Tecnología de Productos Naturales, Tecprona, Departamento de Farmacia, Facultad de Ciencias, Universidad Nacional de Colombia, Cra. 30 No. 45-03, Bogotá, D. C., Colombia. Correo electrónico:
[email protected]. Recibido para evaluación: 19 de noviembre de 2014. Aceptado para publicación: 1º de febrero de 2015. Summary Physalis peruviana is an Andean specie whose fruits are eaten as food and also has been reported in Colombian folk medicine for diabetes mellitus treatment. In addition, previous pharmacological studies on diabetic Wistar rats, an extract of P. peruviana fruits has been showed antidiabetic activity. In order to deepen in P. peruviana action mode as antidiabetic, in this investigation were determinate the Inhibitory Concentrations 50 (IC50) of P. peruviana fruits crude extract on alpha glucosidase from S. cerevisiae and from intestinal rat powder, on maltase and alpha amylase enzymes. The kinetic behavior of the extract on each enzyme was also investigated, and the enzyme constant (Km) and maximum rate (Vmax) were determined. Extract of fruits of P. peruviana showed different IC50 for alpha glucosidase from S. cerevisiae and intestinal rat powder, suggesting greater affinity for the enzyme of mammalian source (4114.7 and 3552.7 µg/mL, respectively). For maltase, the IC50 was close to that obtained for alpha glucosidase (4191.0 µg/mL) while for alpha amylase, the extract exhibited the highest inhibition (IC50: 619.9 g/mL). Regarding kinetic behavior, the extract showed competitive inhibition on alpha-glucosidase and maltase, and on the non-competitive type of alpha amylase. These suggest that inhibition of intestinal carbohydrases is one of the modes of action for the antidiabetic activity of fruits of P. peruviana. 72 cerevisiae y de polvo intestinal de rata. peruviana. el extracto presentó la mayor inhibición (CI50: 619. Además. alpha amylase.0 µg/mL). estudios farmacológicos previos en ratas Wistar han demostrado actividad antidiabética de extractos de frutos de P. mostró diferentes valores de CI50 para alfa glucosidasa obtenida de S. alpha glucosidase. El comportamiento cinético del extracto sobre cada una de las enzimas también fue investigado y la constante enzimática (Km) y la velocidad máxima (Vmax) fueron determinadas. Los resultados sugieren que la inhibición de carbohidrasas intestinales es uno de los modos de acción de los frutos de P.Effects of Physalis peruviana on intestinal carbohydrases Key words: Physalis peruviana. sobre las enzimas alfa glucosidasa obtenida de S. son empleados en la medicina tradicional para el tratamiento de la diabetes mellitus.7 µg/mL. maltasa y alfa amilasa. peruviana. cerevisiae y para la obtenida de polvo intestinal de rata. peruviana.9 g/mL). Para maltasa la CI50 fue cercana a la obtenida para alfa glucosidasa (4191. Respecto al comportamiento cinético. Con el fin de profundizar en el modo de acción de la actividad antidiabética de los frutos de P. en la presente investigación se determinó la concentración inhibitoria 50 (CI50) del extracto crudo de frutos de P.7 and 3552. peruviana como agente antidiabético. mientras para alfa amilasa. Palabras clave: Physalis peruviana. alfa amilasa. carbohidrasas intestinales. respectivamente). cuyos frutos además de ser usados como alimento. Resumen Evaluación in vitro del efecto de un extracto de frutos de Physalis peruviana sobre algunas carbohidrasas intestinales Physalis peruviana es una especie andina. sugiriendo una mayor afinidad por la enzima de origen mamífero (4114. 73 . el extracto mostró inhibición de tipo competitiva sobre alfa glucosidasa y maltasa y no competitiva sobre alfa amilasa. maltase. alfa glucosidasa. El extracto de frutos de P. maltasa. intestinal carbohydrases. peruviana. Luis Fernando Ospina. dysfunction and failure of various organs [1]. and pancreatic transplants [2].. which are converted into monosaccharides (glucose. fructose. and participate in the cleavage of polysaccharides. particularly on plants with the presence of flavonoids. There are different possible modes of action for antidiabetic drugs. The inhibition of this enzyme slows carbohydrate absorption and decreases postprandial blood glucose levels in both normal and diabetic subjects [2]. Currently. Diana Marcela Aragón Introduction Diabetes Mellitus Type II is a metabolic disorder characterized by permanent hyperglycemia. including changes in lifestyle. However. we cannot ignore the scientific and technological advances that have led to a better understanding of the behavior of nature. The use of plants for medicinal purposes comes from our native communities. peruviana. commonly known as “uchuva”. Since fruits of P. one of them is the inhibition of enzymes necessary for polysaccharide digestion (these enzymes are also called carbohydrases). its fruits have shown in vivo antidiabetic activity. many researchers have focused on the search for medicinal plants that inhibit carbohydrases [5-7]. finding valuable information. use of oral hypoglycemic drugs or biotechnology products. 2009 who 74 . where it is passed down from generation to generation. Traditional medicine also plays an important role in the health care of the remaining 20% of the populations of the emerging economies and some developed countries [3]. and it is essential to rigorously investigate the so-called medicinal plants. In addition to its ethnopharmacological use. The World Health Organization has estimated that approximately 80% of the population in emerging countries make regular use of traditional medicine (mostly derived from plants) and primary health care. polyphenols and sugar derivatives [8]. peruviana have these secondary metabolites [9-11] the hypoglycemic effect may be due to inhibition of intestinal carbohydrases such as was reported by Pinto et al. lowering blood glucose levels and some markers of oxidative stress [4]. Chronic hyperglycemia is associated with damage. to determine their safety and effectiveness. They are present in the intestinal villi. In recent years.Diana Patricia Rey. a transmission of knowledge known as ethnomedicine. One of the plants used in traditional medicine for the treatment of diabetes mellitus is P. However. galactose). it has recently been shown that plants play an important role in health care. there are different treatments for diabetes mellitus type II. which is caused by defects in the secretion or action of insulin. peruviana on some intestinal carbohydrases and identify the type of inhibition as possible mode for its hypoglycemic action.25. Maltose Sigma/Aldrich 63418. the percolator was opened and the collected extract was concentrated in a rotary evaporator. porcine pancreatic alpha-amylase (PPA) Sigma/Aldrich A3170. The resulting dry material was milled and was placed in a 2 L percolator to which 1500 mL of 96% ethanol was subsequently added. 6. The volume was then made up 2 mL with distilled water. 100 µL of Folin-Ciocalteu phenol reagent 2N was added to the mixture and shaken.5% Na2CO3 solution was added to the mixture. directly by fruit traders from crops located in Granada-Cundinamarca. peruviana used was prepared as follows: 400 g of fresh fruits were blended with 300 mL of 96% ethanol. cerevisiae) Sigma/Aldrich G5003.Effects of Physalis peruviana on intestinal carbohydrases found that fruits of P. and 50 μg/mL) was added to 2 mL tube. After 24 hours. rat intestinal powder (from acetone) Sigma/Aldrich I1630. Blue Starch Sigma/ Aldrich S7776. LiquiColor a commercial kit (Human GLLQ1).5. The obtained juice was dryed in a circulant air oven at 40 °C for 24 hours. peruviana fruits were collected in February of 2012. 25.13. Preparation of the extract The ethanolic extract of fruits of P. and ethanolic extract of fruits of Physalis peruviana. 12. p-nitrophenyl-α-D-glucopyranoside (pNPG) Sigma/Aldrich N1377. peruviana inhibited the alpha amylase and alpha glucosidase enzymes [11]. the aim of this study was to deepen in the evaluation of in vitro inhibition of the extract of fruits of P. Total phenolic content The total phenolic content were determined by using the Folin-Ciocalteu assay [12]. A reagent blank using distilled water was prepared. Colombia. Plant material The P. After incubation for 120 75 . Methods and materials Materials Alpha-glucosidase derived from Saccharomyces cerevisiae (S. After 5 minutes 200 µL of 7. Thus. Acarbose Sigma/Aldrich A8980. The plant was identified and classified at the Herbario Nacional Colombiano – Universidad Nacional de Colombia and a voucher specimen was deposited in his collection under the code number (COL-574701). An aliquot (100 µL) of extracts or standard solution of gallic acid (3. 10 μL of maltose (7. After centrifugation (15000 rpm. the absorbance against the reagent blank was determined at 726 nm with an UV-Visible spectrophotometer. 10 μL of α-glucosidase (1 UI/ mL. Luis Fernando Ospina. 4 °C) the supernatant was used for the following tests. 17] with slight modifications. 30 min. with slight modifications [13]. changing only the source of alpha-glucosidase. ABlank and ASample are defined as the absorbance of 100% enzyme activity (only the solvent with the enzyme). Inhibition (%) = 100x {( A Background − } ABlank )−( ASample− ABlank ) ( ABackground− ABlank ) (1) Where ABackground. the blank (the test sample without the enzyme) and the test sample (with the enzyme) respectively. 10 μL of pNPG (11. cerevisiae The alpha glucosidase inhibition activity was evaluated by measuring the release of p-nitrophenol from p-nitrophenyl-α-D-glucopyranoside (pNPG) following the method proposed by Pistia-Brueggemann. The assay contained 40 μL of phosphate buffer (0. 15].5 M. peruviana extract or acarbose (positive control) in a range of 20 to 10240 μg/mL. cerevisiae). Inhibition of alpha glucosidase extracted from rat intestinal powder The reaction mixture of this test was conducted under the same test conditions as those described in the previous section.Diana Patricia Rey. which was obtained from acetone extract of rat intestine.9%) and sonicated twelve times for 30 seconds at 4 °C.5 M. The alpha-glucosidase inhibitory activity was calculated according to equation 1. The absorbance was read after incubation for 45 minutes at 37 °C in a BioRad microplate spectrophotometer reader at 550 to 415nm. according to previous works [14. Briefly.8). Diana Marcela Aragón minutes at room temperature. Inhibition of alpha glucosidase derived from S.8). 100 mg of rat intestinal powder was suspended in 1 mL of NaCl (0. Alpha-glucosidase inhibitory activity was calculated according to equation 1. Inhibition of maltase Inhibition of maltase was performed by measuring the release of glucose by the Glucose Oxidase-peroxidase method [16. The assay contained 40 μL of phosphate buffer (0. derived from S.3 mM) and P. Total phenolics content was expressed as mg Gallic Acid Equivalents (mg GA/ g of sample dry weight).5 mM) and 10 μL 76 . pH 6. 10 μL of maltase obtained from acetone extract from rat intestine (1 UI/mL). pH 6. 1 IU/ml) and 200 µL of extract of P.05 M. The statistical calculations and graphs were processed using GraphPad Prism version 5 for Windows. Inhibition of alpha-amylase The alpha-amylase inhibition activity was performed following the methodology based on the hydrolysis of starch covalently linked to Remazol Brilliant Blue [18]. described by Hansawasdi-Kawabata [19] with slight modifications. Next. and were analyzed statistically by the Tukey test and analyzed by two-way ANOVA. All inhibitory concentrations 50 (IC50) were calculated using the GraphPad Prism version 5. except that the substrate concentrations were varied.01 M). The results were used to determine the enzyme constant (Km) and maximum rate (Vmax) [20. The absorbance was read after incubation at 37 °C for 45 minutes in a spectrophotometer with a microplate reader at 540 nm (BIORAD XMark). ranging from 2. For the assay. The reaction was started by adding the enzyme. Statistics analysis The results were expressed as the arithmetic mean values ± standard deviation or standard error of the mean. 100 µL of Tris-HCl buffer (0. 2.2 mM to 16. The maltase inhibitory activity was calculated according to equation 1. The difference between the sample and the target was considered significant (*) when p < 0. and the endpoint was read at 415 nm for alpha-glucosidase. followed by the Bonferroni test for multiple comparisons. peruviana or Acarbose (positive control) in a range of 20 to 10240 μg/mL.Effects of Physalis peruviana on intestinal carbohydrases of the extract of P. 100 µL of porcine pancreatic alpha-amylase (PPA. 77 . peruviana extract on the evaluated enzymes The kinetic behavior of the extract of each enzyme was performed following the methodology described above.9 with calcium chloride 0. The alpha-amylase inhibitory activity was calculated according to equation 1. Absorbance was read after incubation at 37 °C for one hour at 595 nm. 540 nm to 595 nm for maltase and alphaamylase at time intervals of 5 minutes for 20 min. 21] using a linear regression according to Lineweaver-Burk model. in the GraphPad Prism version 5 for Windows Software. The concentration of the extract was held constant to 5120 μg/mL. using a TECAN GENios spectrophotometer. 200µL of Remazol Brilliant Blue (10 mg/mL) was boiled for 5 min. pH 6. peruviana or Acarbose (positive control) in a range of 20 to 10240 μg/mL were added.05.9 mM.00 for Windows software Kinetic behavior of P. 7 3552.(442. 78 .Diana Patricia Rey. cerevisiae and alpha glucosidase extracted from rat intestinal powder are showed in Figures 1 and 2 respectively.0.(2530. peruviana on alpha glucosidase from S. this content is less than that reported by other authors [11]. Luis Fernando Ospina.5. peruviana extract on alpha glucosidase differ according to the source of the enzyme.2 4114. Inhibitory activities of an extract of fruits of P.0. P.0 229.6 619.(2826.0.0.7 570. cerevisiae: Saccharomyces cerevisiae – P. Table 1. The IC50 values found are reported in the Table 1. Inhibitory activity of P. peruviana fruits are rich in phenolic compounds.4) 5896.7 263. it was found that employed extract content 6.8 mg GAE/g extract. P.5 4191. it is lower when the enzyme is extracted from the intestinal powder.3 ± 0.(191.7) 704.7) 7277.2mL) 1296. peruviana: Physalis peruviana.0) 5990. [11] (ethanol 12%).(457. It can be explained since the solvent used in this investigation (ethanol 96%) is less polar that that the solvent used by Pinto et al. Diana Marcela Aragón Results Total phenolic content Previous works have been demonstrated that P.0) 249.(2176. Inhibitor Acarbose peruviana Acarbose peruviana Acarbose peruviana Acarbose peruviana Extract Extract Extract Extract 773.0) IC50: Inhibitory concentration 50 – S. peruviana on alpha glucosidase.5. peruviana on alpha glucosidase. cerevisiae Alpha glucosidase extracted from rat intestinal powder Maltase extracted Alpha amylase from from rat intestinal porcine pancreas powder P.0) 407.0) 691.1. The IC50 are expressed as the mean and the confidence limits of 95%.(153. It is important to note that the IC50 of acarbose and P. In this investigation.9 IC50 (µg/ (470. maltase and alpha amylase The inhibition activities of P. P. maltase and alpha amylase Enzyme Alpha glucosidase Source from S. Effects of Physalis peruviana on intestinal carbohydrases 80 % Inhibition 60 40 20 0 2 3 4 log (inhibitor) P. peruviana Acarbose Figure 1. Results are expressed as mean ± SEM (n = 3). Inhibitory activity of an extract of fruits of P. 100 % Inhibition 80 60 40 20 0 2 3 4 log (inhibitor) Acarbose P. cerevisiae. peruviana on alpha glucosidase from lyophilized rat intestinal powder. 79 . Inhibitors: Acarbosa and ethanolic extract of fruits P. peruviana Figure 2. Results are expressed as mean ± SEM (n = 3). Inhibitory activity of an extract of fruits of P. Inhibitors: Acarbosa and ethanolic extract of fruits P. peruviana. peruviana. peruviana on alpha glucosidase from S. 100 % Inhibition 80 60 40 20 0 2 3 4 log (inhibitor) Acarbose P. peruviana on alpha glucosidase from S.Diana Patricia Rey. Inhibitors: Acarbosa and ethanolic extract of fruits P. Luis Fernando Ospina. peruviana extract is very close to that found on alpha glucosidase from S. the lowest IC50 obtained was for P. peruviana on maltase. cerevisiae. The IC50 of acarbose on this enzyme is lower than on alpha glucosidase (less than half ) while the IC50 of P. peruviana. peruviana on maltase is shown in Figure 3. peruviana on alpha-glucosidase. Results are expressed as mean ± SEM (n = 3). peruviana. and the kinetic parameters are presented in Table 2. peruviana extract has a competitive-type behavior on inhibition of and maltase where the presence of the substrate reduces the inhibitory activity of the extract but not change the maximum rate while it was found a mixed type inhibition on alpha-glucosidase. Inhibitory activity of an extract of fruits of P. P. and the IC50 value found is shown in Table 1.The inhibitory activity of the extract of P. peruviana is shown in Figure 4. peruviana extract on the evaluated enzymes The reaction rates of P. maltase and alpha amylase are shown in Figures 5 to 7. For alpha amylase. Inhibitors: Acarbosa and ethanolic extract of fruits P. Inhibitory activity of an extract of fruits of P. peruviana. the inhibitory activity of P. and slightly higher than those obtained on the extracted alpha glucosidase. peruviana Figure 3. cerevisiae. Diana Marcela Aragón Figure 1. Results are expressed as mean ± SEM (n = 3). The IC50 value is lower than that found on alpha glucosidase and maltase (Table 1). since 80 . Kinetic behavior of P. 569 0. kinetic constant. peruviana extract Without inhibitor P.087 0. 81 . peruviana extract Without inhibitor P. Kinetic parameters of the inhibition of the extract from P. peruviana on the different enzymes. Maximum rate – Km.538 3. Inhibitors: Acarbosa and ethanolic extract of fruits P.707 Type of inhibition Mixed Competitive Non-Competitive Vmax.411 Vmax (mM/min) 0.512 71.032 1098.009 0.526 115. peruviana Acarbose Figure 4. Table 2. Inhibitory activity of an extract of fruits of P. Alpha glucosidase Maltase Alpha amylase Without inhibitor P.654 118. peruviana extract Km 1. Regarding alpha amylase.877 458.007 0.009 0. P.011 0. 120 % Inhibition 100 80 60 40 20 0 2 3 4 log (inhibitor) P.Effects of Physalis peruviana on intestinal carbohydrases the maximum rate (Vmax) is reduced and the enzyme constant (Km) is increased.004 Km/ Vmax 137.205 1. Results are expressed as mean ± SEM (n = 3). peruviana.110 7. peruviana on alpha amylase.008 0. peruviana extract exhibited a non-competitive behavior on this enzyme. 4 1/[pNG(mM)] P.0.1. 82 .0. . peruviana.6 .0. V.0.Diana Patricia Rey.0. peruviana Without inhibitor Figure 5. Reaction rate of alpha-glucosidase on pNPG in the presence and absence of the ethanolic extract of fruits of P.0. reaction rate 700 1/V (mM/min) 600 400 400 300 200 100 .6 .2 0.0 .4 . Luis Fernando Ospina.2 0.4 .2 . Reaction rate of maltase on maltose in the presence and absence of ethanolic extract of fruits of P. pNPG (p-nitrophenyl-α-D-glucopyranoside).4 1/[Maltose(mM)] Without inhibitor P. Diana Marcela Aragón 700 1/V (mM/min) 400 300 200 100 .0.8 .2 0. peruviana.1.0 .0.0 0.0 . peruviana Figure 6.0. not reported IC50 values. For these plants. cerevisiae (4. This concentration is higher than the IC50 finding in this investigations. This is not the case with P. peruviana on alpha glucosidase.2 mg/mL for extract of Andrographis paniculata Nees [23]. is possible to note that inhibitions near to 50% was achieve with concentration more than 10 mg/mL of P. peruviana.11mg / mL) was high but similar to the IC50 presented by other extracts of medicinal plants traditionally used as hypoglycemiants. which suggests that 83 . Discussion Inhibitory activity of P. Previous works had reported that the most of the plant extracts have lower IC50 on alpha-glucosidase extracted from S.Effects of Physalis peruviana on intestinal carbohydrases 400 300 1/V (mM/min) 200 100 -3 -2 1 -1 2 -100 1/[Azure Starch(mg/mL)] Without inhibitor P. Reaction rate of alpha-amylase on azure starch in the presence and absence of the ethanolic extract of fruits of P.. IC50 values have been reported ranging from 1. beside the lower content of total phenolic compounds in our extract.8 µg/mL for Punica granatum extract [22] to 17. in spite of Pinto et al. On the other hand. peruviana. maltase and amylase The IC50 found for P. These findings suggest that other compounds besides phenols could be responsible of the alpha glucosidase inhibition. cerevisiea than on the enzyme extracted from mammalian intestine [24-26]. peruviana fruits extract [11]. peruviana on alpha glucosidase from S. peruviana Figure 7. For alpha amylase. cerevisiae [26.Diana Patricia Rey. cerevisiae do not show inhibition on alpha glucosidase extracted from mammals [15. peruviana on maltose is consistent with the results obtained in the inhibition. such as Stichopus japonicus [29]. it was found a 84 . but no inhibitory activity against alpha glucosidase form S. This may be because the extract has a large number of compounds that can bind to various proteins contained in the crude enzyme solution. a drug that has a competitive type of inhibition of these enzymes. and diarrhea [15]. For the enzyme maltase on acarbose. Thus. This fact is important because a plant extract capable of inhibiting the digestion of complex carbohydrates in the human gastrointestinal tract should show inhibition of the enzyme extracted from the mammal. peruviana extract on the evaluated enzymes The kinetic behavior of P. although P. since the extract behaved very similarly to acarbose. peruviana. 30]. not only the enzyme obtained from microorganisms. the IC50 values found were lower. Similar to reported for alpha glucosidase.9 and 229. 27]. since the values reported for inhibition of alpha glucosidase obtained from microorganisms cannot be extrapolated to enzymes from mammalian intestine. peruviana IC50 was higher than acarbose IC50 (619. making its binding less specific. Pinto et al. respectively). Thus. Some authors report that both acarbose and voglibose have high inhibitory effects of alpha glucosidase in mammals. almost 100 times more than the IC50 found in this investigation [11]. the IC50 was not significantly different from the IC50 on alpha glucosidase. In the case of the ethanolic extract of fruits of P. Luis Fernando Ospina. This divergence may be due to the difference in binding site molecular recognition of enzymes. Kinetic behavior of P. 31] are related to some side effects such as flatulence and bloating. suggesting that the extract of P. Diana Marcela Aragón this extract is more specific for mammalian intestinal enzymes. peruviana produces a strong inhibition of this enzyme. a lower IC50 was found than on alpha glucosidase. found 65% as the maximum inhibition when it was tested P. The strong inhibition of acarbose on alpha amylase and lack of digestion of starch [30. many inhib itors of alpha glucosidase from S. an extract that shows less inhibition on alpha amylase could minimize these side effects [25. This is because acarbose binds to the enzyme with higher affinity than the substrate itself [28]. For alpha glucosidase.6 µg/mL. 27]. This fact had also been reported in other extracts. peruviana extract at concentration of 50 mg/mL. and the high inhibition on alpha-amylase. peruviana has shown different responses to microbial alpha glucosidase (Type I) and alpha glucosidase extracted from rat intestinal powder (Type II). or for which biological studies have demonstrated antioxidant activity. 34].Effects of Physalis peruviana on intestinal carbohydrases mixed type inhibition such as it was reported for some flavonoids especially quercetin [32]. resulting in less interaction with meals [26. 85 . could be responsible for the moderate inhibition on alpha glucosidase. Likewise. it is possible for one inhibitor to bind to the active region of alpha-glucosidase and another to bind to the active region of alpha amylase. the findings of this investigation suggested that not only phenolics compounds but others. Declaration of interest The authors report no declarations of interest. such as flavonoids. peruviana extract is the fact that the extract presents more than one inhibitor. including quercetin. 33. Based on the results of this investigation. Flavonoids or phenolic compounds have been linked to the inhibition of alpha-glucosidase and alpha-amylase [36]. is important to note that non-competitive behavior is usually preferred. Another factor that may explain the combination of competitive and non-competitive inhibition on the evaluated enzymes presented by P. are promising in inhibiting alpha-glucosidase and amylase. 39]. and on the non-competitive type of alpha amylase. However. a flavonoid described for Physalis peruviana fruits [11]. it is suggested that inhibition of intestinal carbohydrases is one of the modes of action by which the fruits of P. the extract exhibited a non-competitive inhibition that may be related to structural differences due to the origins of the enzymes [35]. Conclusions Ethanolic extract of fruits of P. peruviana type shows competitive inhibition on alpha-glucosidase. ethanol extract of fruits of P. because this prevents the presence or absence of substrate from affecting the binding of the inhibitor to the enzyme. peruviana exert hypoglycemic and antidiabetic activity. Regarding to alpha amylase. Due to the presence of polyphenols. the presence of both flavonoids and other phenols has been reported [37]. For fruits of P. and plants with phytochemical studies that have reported the presence of these secondary metabolites. However. peruviana. campferol and flavonols [38. Prasad-Kota. fruit at two maturity stages.P. Kwon. Cassia auriculata. Mc-Graw Hill Interamericana Editores. S. Önal. Ospina. J.I. 4. Supercritical carbon dioxide extract of Physalis peruviana induced cell cycle arrest and apoptosis in human lung cancer H661 cells.S. 1132 (2010). Y. Matsui. 2541 (2004). S. D. S.L.C. 35. Licodiedoff.. México DF. R. Hou. Fauci . L.L. Galvez. 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