Inhibitory effect of 0.19 AI inhibitor from wheat kernel on the activity and stability of porcine pancreas alpha-amylase

CFW Plexus ◽  
2012 ◽  
Author(s):  
Kennichi Asada
Keyword(s):  
Inhibitory Effect ◽  
Alpha Amylase ◽  
Porcine Pancreas ◽  
Wheat Kernel

scholarly journals Alpha-Amylase Inhibitory Effect and Docking Studies of Some New Curcumin-Triazole Derivatives

2019 ◽  
Vol 3 (11) ◽  
pp. 124-129
Author(s):  
Eman Elattar ◽  
Amal A Galala ◽  
Hassan -Elrady A Saad ◽  
Farid A Badria
Keyword(s):  
Inhibitory Effect ◽  
Docking Studies ◽  
Alpha Amylase ◽  
Triazole Derivatives

scholarly journals Structural studies of wheat monomeric and dimeric protein inhibitors of α-amylase

1978 ◽  
Vol 173 (1) ◽  
pp. 229-235 ◽  
Author(s):  
T Petrucci ◽  
G Sannia ◽  
R Parlamenti ◽  
V Silano
Keyword(s):  
Alpha Amylase ◽  
Protein Inhibitors ◽  
Inhibitor Molecule ◽  
Wheat Kernel ◽  
Electrophoretic Mobilities ◽  
Structural Equivalence ◽  
Phylogenetic Origin ◽  
The Common ◽  
Dimeric Protein ◽  
Amylase Inhibitors

Two wheat monomeric protein inhibitors of alpha-amylase with mol.wt. 12000, designated inhibitors 0.28 and 0.39 according to their gel-electrophoretic mobilities, showed almost identical circular-dichroism spectra in both the far and near u.v. at different pH values as well as in the presence or absence of dissociating and reducing agents. Both inhibitors (0.28 and 0.39) were readily inactivated by reduction of the five disulphide bridges present in each inhibitor molecule. These properties are very similar to those exhibited by the wheat dimeric protein inhibitor of alpha-amylase with mol.wt. 24000, designated inhibitor 0.19 according to its gel-electrophoretic mobility. The N-terminal sequence of the 0.19 inhibitor was determined without separating its subunits and compared with that of the 0.28 inhibitor reported by Redman [(1976) Biochem. J. 155, 193–195]. Petide ‘maps’ from tryptic digests of reduced and carboxymethylated inhibitors 0.19 and 0.28 were compared. One molecule of reducing sugar is covalently bound per inhibitor-0.19 protomer and inhibitor-0.28 molecule. The results obtained strongly support previous findings indicating the structural equivalence of inhibitor 0.28 with each inhibitor-0.19 protomer and the common phylogenetic origin of these protein alpha-amylase inhibitors from wheat kernel.

Inhibitory effect of 4,4′-[ethane-1,2-diylbis(sulfandiylmethanediyl)]bis(3,5-dimethyl-1H-pyrazole) and its derivatives on alpha-amylase activity

2016 ◽  
Vol 25 (7) ◽  
pp. 1384-1389 ◽  
Author(s):  
Vadim Maksimov ◽  
Radik Zaynullin ◽  
Nail Akhmadiev ◽  
Elda P. Segura-Ceniceros ◽  
José L. Martínez Hernández ◽  
...  
Keyword(s):  
Amylase Activity ◽  
Inhibitory Effect ◽  
Alpha Amylase

scholarly journals IN VITRO ANTIDIABETIC POTENTIALS OF SIDA ACUTA, ABUTILON INDICUM AND MALVASTRUM COROMANDELIANUM

2020 ◽  
pp. 87-89
Author(s):  
NANTAPORN DINLAKANONT ◽  
CHANIDA PALANUVEJ ◽  
NIJSIRI RUANGRUNGSI
Keyword(s):  
Enzyme Inhibitors ◽  
Postprandial Glucose ◽  
Inhibitory Effect ◽  
Glucose Absorption ◽  
Alpha Amylase ◽  
Sida Acuta ◽  
Inhibitory Activities ◽  
Alpha Glucosidase ◽  
Abutilon Indicum

Objective: Starch metabolizing enzyme inhibitors are able to retard postprandial glucose absorption. This study aimed to investigate the in vitro inhibitory activities of alpha-glucosidase and alpha-amylase of three Malvaceous weeds i.e. Sidaacuta Burm. f., Abutilon indicum (Linn.) Sweet and Malvastrumcoromandelianum (Linn.) Garcke. Methods: The stems, roots and leaves of S. acuta, A. indicum and M. coromandelianum were sequentially extracted in dichloromethane and methanol, respectively. All fractions were tested for the inhibitory activities on yeast alpha-glucosidase, rat intestinal alpha-glucosidase and porcine alpha-amylase. p-Nitrophenyl-α-D-glucopyranoside and 2-chloro-4 nitrophenol-α-D- maltotrioside were used as the substrate for glucosidase and amylase respectively. Results: The dichloromethane fraction of the roots and stems from A. indicum and dichloromethane as well as methanolic fractions of the stems of M. coromandelianum could inhibit yeast alpha-glucosidase compared to 1-deoxynojirimycin with the IC50 of 0.36, 0.45, 0.48, 0.48 and 0.58 mg/ml respectively. A. indicum root methanolic fraction had the highest inhibitory effect on rat alpha-glucosidase activity compared to 1-deoxynojirimycin with the IC50 of 0.08 and 0.11 mg/ml respectively. M. coromandelianum, the dichloromethane fraction of roots and the methanolic fraction of stems, showed the strongest effect on alpha-amylase inhibition compared to acarbose with the IC50 of 0.07, 0.07 and 2.7 mg/ml, respectively. Conclusion: S. acuta, A. indicum and M. coromandelianum dichloromethane and methanolic fractions of the root, stem and leaf parts demonstrated an appreciable inhibitory activity on alpha-amylase from porcine, alpha-glucosidase from Saccharomyces cerevisiae and from rat intestine compared to 1-deoxynojirimycin and acarbose.

scholarly journals Assessment of In Vitro Antidiabetic Potential of Purified Anthocyanin Extract from Floral Petals of Wild Balsam Species

2020 ◽  
Vol 10 (3) ◽  
pp. 31-35
Author(s):  
R ARATHY ◽  
K MURUGAN ◽  
KV DINESH BABU ◽  
GS MANOJ
Keyword(s):  
International Diabetes Federation ◽  
Inhibitory Effect ◽  
Alpha Amylase ◽  
Herbal Remedies ◽  
Antidiabetic Activity ◽  
Public Health Issue ◽  
Impatiens Balsamina ◽  
Alpha Glucosidase

Diabetes is a notorious and growing clinical and public health issue. The International Diabetes Federation assumes that 592 million had diabetes by 2035 and that by 2040 the number will increase to 642 million. Cardiovascular corollary accounts for four million deaths annually attributable to diabetes. Evidence reveals that certain glucose-lowering phytochemicals can improve vascular outcomes with type 2 diabetes, which, together with better understanding of using multiple therapies concurrently, offers opportunities for beneficial personalization of medication regimens. Anthocyanins are coloured pigments and are natural antioxidants. Keeping this in focus, this study was undertaken to evaluate the in vitro antidiabetic activity in the petals of wild Impatiens balsamina L. The anthocyanin was extracted from floral petals of wild balsam species and purified to homogeneity using chromatographic techniques. Evaluation of in vitro antidiabetic properties of anthocyanin extract revealed a dose-dependent increase in the inhibitory effect on the alpha-glucosidase (200 μg/ml) and alpha-amylase enzymes (500 μg/ml) and was comparable with the standard acarbose drug (189 μg/ml and 50 μg/ml). These results indicated that anthocyanin could be used as a source of functional food and nutraceuticals. This information from wild species will be useful in finding more potent antidiabetic principle from the natural resources for the clinical development of antidiabetic therapeutics. Future studies are planned to substantiate the antidiabetic power of anthocyanin using in vivo animal models. Keywords: Alpha amylase, alpha glucosidase, diabetes, herbal remedies, Impatiens balsamina L.

scholarly journals INHIBITORY EFFECT OF A STANDARDIZED HYDROETHANOLIC EXTRACT OF TERMINALIA ARJUNA BARK ON ALPHA-AMYLASE ENZYMEINHIBITORY EFFECT OF A STANDARDIZED HYDROETHANOLIC EXTRACT OF TERMINALIA ARJUNA BARK ON ALPHA-AMYLASE ENZYME

2018 ◽  
Vol 11 (4) ◽  
pp. 366 ◽  
Author(s):  
Sushant A Shengule ◽  
Sanjay Mishra ◽  
Shweta Bodhale
Keyword(s):  
Inhibitory Activity ◽  
High Performance ◽  
Soxhlet Extraction ◽  
Inhibitory Effect ◽  
Alpha Amylase ◽  
Antidiabetic Activity ◽  
Bark Extract ◽  
Terminalia Arjuna ◽  
Hydroethanolic Extract

 Objective: The present study was initiated to screen the hydroethanolic bark extract for α-amylase inhibitory activity and standardization of the Terminalia arjuna for polyphenolic phytochemicals using high-performance liquid chromatography-photo diode array (HPLC-PDA) method.Methods: The T. arjuna bark sample was extracted with ethanol: water (70:30 v/v) using Soxhlet extraction. A Dionex P680 HPLC system was used to acquire chromatograms. The screening of extract of T. arjuna bark has performed for in vitro α-amylase inhibitory assay. Each experiment was repeated 3 times. All values were expressed mean ± standard deviation.Results: The content of arjunetin, arjungenin, gallic acid, ellagic acid, and quercetin was 0.47, 8.22, 2.443, 7.901, and 3.20 mg/g, respectively, in a hydroethanolic extract of T. arjuna. The hydroethanolic extract of T. arjuna bark and acarbose has shown an inhibitory activity with an IC50 value 145.90 and 62.35 μg/mL, respectively.Conclusion: The hydroethanolic extract T. arjuna bark demonstrates α-amylase inhibitory activity due to a synergistic effect of the phytochemical constituents present in it. This study suggests that one of the mechanisms of this plant for antidiabetic activity is through the inhibition of α-amylase enzyme.

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