scholarly journals Studies on the Amylase Inhibitors from the Seeds of Adenanthera Pavonina

2017 ◽  
Vol 14 (3) ◽  
pp. 1009-1015
Author(s):  
K.S. Chandrashekharaiah
Keyword(s):  
Specific Inhibitor ◽  
Gel Permeation Chromatography ◽  
Zone Of Inhibition ◽  
Adenanthera Pavonina ◽  
Amylase Inhibitor ◽  
Heat Stable ◽  
Optimum Ph ◽  
Ammonium Sulphate Fractionation ◽  
Treatment Of Diabetes ◽  
Amylase Inhibitors

ABSTRACT: An α-Amylase inhibitor was isolated and purified employing ammonium sulphate fractionation, molecular sieve chromatography on sephadex G-10 and G-50 and HPLC from the seeds of Adenanthera pavonina. The molecular weight was found to be 10 - 12 kDa as determined by gel-permeation chromatography on Sephadex G-100. The specific inhibitor activity, fold purity and the yield obtained for Adenanthera pavonina amylase inhibitor was 32.12, 51 and 13.07, respectively. The purified inhibitor was heat stable and retained more than 52% activity at 65°C. The optimum pH obtained for purified inhibitor was 6.3 and 100% Zone of inhibition was observed when it was added on the plated organisms. The Adenanthera pavonina amylase inhibitor inhibited the activity of human salivary α-amylase and inhibitory activity of α-amylase inhibitor against mammalian amylases could suggest its potential in treatment of diabetes and related nutritional problems results in obesity.

Structure-based design of human pancreatic amylase inhibitors from the natural anthocyanin database for type 2 diabetes

2020 ◽  
Vol 11 (4) ◽  
pp. 2910-2923 ◽  
Author(s):  
Lianghua Xie ◽  
Jianling Mo ◽  
Jingdan Ni ◽  
Yang Xu ◽  
Hongming Su ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Design Approach ◽  
Pancreatic Amylase ◽  
Amylase Inhibitor ◽  
Amylase Inhibitors

Malvidin 3-O-arabinoside is identified as a novel human pancreatic amylase inhibitor from the natural anthocyanin database with a structure-based design approach.

Amylase inhibitors ofActiniae of the Caribbean Sea amylase inhibitor of protein nature fromStoichactis helianthus

1982 ◽  
Vol 18 (3) ◽  
pp. 317-322
Author(s):  
T. N. Zvyagintseva ◽  
V. V. Sova ◽  
I. Perera ◽  
L. A. Elyakova
Keyword(s):  
Caribbean Sea ◽  
Amylase Inhibitor ◽  
Protein Nature ◽  
The Caribbean ◽  
Amylase Inhibitors

scholarly journals Mutants of common bean alpha-amylase inhibitor-2 as an approach to investigate binding specificity to alpha-amylases

2004 ◽  
Vol 39 (3) ◽  
pp. 201-208 ◽  
Author(s):  
Maria Cristina Mattar da Silva ◽  
Luciane Vieira Mello ◽  
Marise Ventura Coutinho ◽  
Daniel John Rigden ◽  
Goran Neshich ◽  
...  
Keyword(s):  
Phaseolus Vulgaris ◽  
Inhibitory Activity ◽  
Molecular Basis ◽  
Tobacco Plants ◽  
Defense Proteins ◽  
Amylase Inhibitor ◽  
Terminal Loop ◽  
Stored Grains ◽  
Alpha Amylase Inhibitor ◽  
Amylase Inhibitors

Despite the presence of a family of defense proteins, Phaseolus vulgaris can be attacked by bruchid insects resulting in serious damage to stored grains. The two distinct active forms of a-amylase inhibitors, a-AI1 and a-AI2, in P. vulgaris show different specificity toward a-amylases. Zabrotes subfasciatus a-amylase is inhibited by a-AI2 but not by a-AI1. In contrast, porcine a-amylase is inhibited by a-AI1 but not by a-AI2. The objective of this work was to understand the molecular basis of the specificity of two inhibitors in P. vulgaris (a-AI1 and a-AI2) in relation to a-amylases. Mutants of a-AI2 were made and expressed in tobacco plants. The results showed that all the a-AI2 mutant inhibitors lost their activity against the insect a-amylases but none exhibited activity toward the mammalian a-amylase. The replacement of His33 of a-AI2 with the a-AI1-like sequence Ser-Tyr-Asn abolished inhibition of Z. subfasciatus a-amylase. From structural modeling, the conclusion is that the size and complexity of the amylase-inhibitor interface explain why mutation of the N-terminal loop and resultant abolition of Z. subfasciatus a-amylase inhibition are not accompanied by gain of inhibitory activity against porcine a-amylase.

scholarly journals Antidiabetic Indian Plants: A Good Source of Potent Amylase Inhibitors

2011 ◽  
Vol 2011 ◽  
pp. 1-6 ◽  
Author(s):  
Menakshi Bhat ◽  
Smita S. Zinjarde ◽  
Shobha Y. Bhargava ◽  
Ameeta Ravi Kumar ◽  
Bimba N. Joshi
Keyword(s):  
Chloroform Extract ◽  
Physiological Factors ◽  
Enzyme Preparations ◽  
Diabetes Type Ii ◽  
Eugenia Jambolana ◽  
Glucosidase Inhibitors ◽  
Bougainvillea Spectabilis ◽  
Treatment Of Diabetes ◽  
Intestinal Glucosidases ◽  
Amylase Inhibitors

Diabetes is known as a multifactorial disease. The treatment of diabetes (Type II) is complicated due to the inherent patho-physiological factors related to this disease. One of the complications of diabetes is post-prandial hyperglycemia (PPHG). Glucosidase inhibitors, particularlyα-amylase inhibitors are a class of compounds that helps in managing PPHG. Six ethno-botanically known plants having antidiabetic property namely,Azadirachta indicaAdr. Juss.;Murraya koenigii(L.) Sprengel;Ocimum tenuflorum(L.) (syn:Sanctum);Syzygium cumini(L.) Skeels (syn:Eugenia jambolana);Linum usitatissimum(L.) andBougainvillea spectabiliswere tested for their ability to inhibit glucosidase activity. The chloroform, methanol and aqueous extracts were prepared sequentially from either leaves or seeds of these plants. It was observed that the chloroform extract ofO. tenuflorum; B. spectabilis; M. koenigiiandS. cuminihave significantα-amylase inhibitory property. Plants extracts were further tested against murine pancreatic, liver and small intestinal crude enzyme preparations for glucosidase inhibitory activity. The three extracts ofO. tenuflorumand chloroform extract ofM. koenigishowed good inhibition of murine pancreatic and intestinal glucosidases as compared with acarbose, a known glucosidase inhibitor.

scholarly journals AKTIVITAS AMILASE, LIPASE DAN PROTEASE DARI CACING Peryonix excavatus

Molekul ◽  
2009 ◽  
Vol 4 (2) ◽  
pp. 115
Author(s):  
Ari Asnani ◽  
Puji Lestari
Keyword(s):  
Enzymatic Activity ◽  
Ammonium Sulphate ◽  
Crude Extract ◽  
Isolation Procedure ◽  
Optimum Temperature ◽  
Enzymes Activities ◽  
Optimum Ph ◽  
Ammonium Sulphate Fractionation

The ability of Peryonix excavatus to live in extremely dirty area indicates that P. excavatus secretes distinctive enzymes which might be useful for industry. Thus, this research were aimed to isolate amylase, lipase and protease from P. excavatus, and to characterize the enzymes to know the optimum temperature and pH. The isolation procedure consisted of extraction and ammonium sulphate fractionation. The results showed that crude extract and ammonium sulphate fractions of P.excavatus had amylase, lipase, and protease enzymes activities. Among the three enzymes, amylase had the highest enzymatic activity whereas lipase was the least. The optimum temperature of amylase, lipase and protease were 60, 40, and 60 oC, respectively. The optimum pH of amylase, lipase and protease were 7, 7, and 8, respectively.

Digestive α-amylases from Tecia solanivora larvae (Lepidoptera: Gelechiidae): response to pH, temperature and plant amylase inhibitors

2008 ◽  
Vol 98 (6) ◽  
pp. 575-579 ◽  
Author(s):  
A. Valencia-Jiménez ◽  
J.W. Arboleda V ◽  
A. López Ávila ◽  
M.F. Grossi-de-Sá
Keyword(s):  
Amylase Activity ◽  
Insect Pest ◽  
Biochemical Properties ◽  
Alpha Amylase ◽  
Isoelectric Points ◽  
Optimum Ph ◽  
Tecia Solanivora ◽  
Alpha Amylase Inhibitor ◽  
Amylase Inhibitors ◽  
Genetically Modified Potatoes

AbstractThe biochemical properties of the digestive alpha-amylase from Tecia solanivora larvae, an important and invasive insect pest of potato (Solanum tuberosum), were studied. This insect has three major digestive α-amylases with isoelectric points 5.30, 5.70 and 5.98, respectively, which were separated using native and isoelectric focusing gels. The alpha-amylase activity has an optimum pH between 7.0 and 10.0 with a peak at pH 9.0. The enzymes are stable when heated to 50°C and were inhibited by proteinaceous inhibitors from Phaseolus coccineus (70% inhibition) and P. vulgaris cv. Radical (87% inhibition) at pH 6.0. The inhibitors present in an amaranth hybrid inhibited 80% of the activity at pH 9.0. The results show that the alpha-amylase inhibitor from amaranth seeds may be a better candidate to make genetically-modified potatoes resistant to this insect than inhibitors from common bean seeds.

scholarly journals Brain arylamidase. Purification and characterization of the soluble bovine enzyme

1969 ◽  
Vol 112 (3) ◽  
pp. 335-342 ◽  
Author(s):  
A. S. Brecher ◽  
J. B. Suszkiw
Keyword(s):  
Soluble Fraction ◽  
Substrate Inhibition ◽  
Gel Filtration ◽  
Bovine Brain ◽  
Purification And Characterization ◽  
Sephadex Column ◽  
Optimum Ph ◽  
Ammonium Sulphate Fractionation ◽  
High Concentrations

1. An enzyme acting on aminoacyl-β-naphthylamides has been isolated from the soluble fraction of bovine brain and purified 205-fold by means of ammonium sulphate fractionation, hydroxyapatite adsorption and DEAE-Sephadex column chromatography. 2. Arylamidase requires thiol groups for retention of its activity, is heat-labile and is susceptible to freezing. p-Chloromercuribenzoate and N-ethylmaleimide inactivate the enzyme rapidly. 3. Metal ions are not required for its activity, but stimulation by Mn2+ and Mg2+ and inactivation by Co2+ and Zn2+ are observed. 4. Optimum pH7·5 in phosphate buffer was exhibited for all substrates tested except l-leucyl-β-naphthylamide, for which optimum pH is 6·5. 5. Km values for a number of substrates have been obtained and substrate inhibition at high concentrations was demonstrated. 6. The molecular weight is approx. 70000 as determined by Sephadex-gel filtration.

Purification and partial biochemical–genetic characterization of trehalose 6-phosphate synthase from muscles of adult femaleAscaris suum

2012 ◽  
Vol 87 (2) ◽  
pp. 212-221 ◽  
Author(s):  
M. Dmitryjuk ◽  
M. Dopieralska ◽  
E. Łopieńska-Biernat ◽  
R.J. Frączek
Keyword(s):  
Genetic Characterization ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Sds Page ◽  
Optimum Ph ◽  
Genes Encoding ◽  
Ammonium Sulphate Fractionation ◽  
Biochemical Genetic

AbstractTrehalose 6-phosphate (T6P) synthase (TPS;EC2.4.1.15) was isolated from muscles ofAscaris suumby ammonium sulphate fractionation, ion-exchange DEAE SEPHACELTManion exchanger column chromatography and Sepharose 6B gel filtration. On sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS–PAGE), 265-fold purified TPS exhibited a molecular weight of 66 kDa. The optimum pH and temperature of the purified enzyme were 3.8–4.2 and 35°C, respectively. The isoelectric point (pI) of TPS was pH 5.4. The studied TPS was not absolutely substrate specific. Besides glucose 6-phosphate, the enzyme was able to use fructose 6-phosphate as an acceptor of glucose. TPS was activated by 10 mMMgCl2, 10 mMCaCl2and 10 mMNaCl. In addition, it was inhibited by ethylenediaminetetra-acetic acid (EDTA), KCl, FeCl3and ZnCl2. Two genes encoding TPS were isolated and sequenced from muscles of the parasite. Complete coding sequences fortps1(JF412033.2) andtps2(JF412034.2) were 3917 bp and 3976 bp, respectively. Translation products (AEX60788.1 and AEX60787.1) showed expression to the glucosyltransferase-GTB-type superfamily.

Bioassay-Guided Separation of an α-Amylase Inhibitor Anthocyanin from Vaccinium arctostaphylos Berries

2010 ◽  
Vol 65 (9-10) ◽  
pp. 567-570 ◽  
Author(s):  
Bahman Nickavar ◽  
Gholamreza Amin
Keyword(s):  
Diabetes Mellitus ◽  
Medicinal Plant ◽  
Inhibitory Effect ◽  
Natural Sources ◽  
Amylase Inhibitor ◽  
Treatment Of Diabetes ◽  
Dose Dependent

Vaccinium arctostaphylos is a traditional medicinal plant in Iran used for the treatment of diabetes mellitus. In our search for antidiabetic compounds from natural sources, we found that the extract obtained from V. arctostaphylos berries showed an inhibitory effect on pancreatic α-amylase in vitro [IC50 = 1.91 (1.89 -1.94) mg/mL]. The activity-guided purification of the extract led to the isolation of malvidin-3-O-β-glucoside as an α-amylase inhibitor. The compound demonstrated a dose-dependent enzyme inihibitory activity [IC50 = 0.329 (0.316 - 0.342) mM].

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