α-amylase inhibitors from wheat: Amino acid sequences and patterns of inhibition of insect and human α-amylases

Feng, Guo Hua; Richardson, Michael; Chen, Ming Shun; Kramer, Karl J.; Morgan, Thomas D.; Reeck, Gerald R.

doi:10.1016/0965-1748(95)00087-9

Cited by 99 publications

(73 citation statements)

References 24 publications

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“…Availability of energy from the dietary legumes is, therefore, dependent to a significant extent on the contents as well as digestibility of carbohydrates in these foods. Starch in legumes possesses low digestibility due to presence of a number of antinutritional factors, such as alpha-amylase inhibitors (Mulimani and Supriya, 1993;Feng et al, 1996). Other antinutrients like phytic acid, saponin and polypheriols also have significant effect on the digestibility of legumes (Kataria et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

Studies on Vigna mango L. - Effect of Processing on Carbohydrate Fractionation and Influence of Grain Starch on Protein Utilization in Albino Rats

Jamil¹,

Bashir²,

Yaqoob³

1999

Pakistan J. of Biological Sciences

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The effect of black gram starch on the utilization of casein was also tested in albino rats using PER, digestibility coefficient, biological value and net protein utilization as parameters. Soaking reduced the levels of sugars, starch and oligosaccharides but starch digestibility was improved significantly. Cooking increased the level of sugars while starch and verbascose content was decreased. Starch digestibility was also improved on cooking. Stachyose and raffinose contents were increased when unsoaked seeds were cooked, but decreased when the seeds were soaked before cooking. Germination decreased starch and oligosaccharide contents thereby raising the level of the soluble sugars. Starch digestibility was increased appreciably on germination. On cooking, the black gram starch promoted growth similar to corn starch as no difference was noticed in the parameters studied in albino rats.

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Section: Introductionmentioning

confidence: 99%

Studies on Vigna mango L. - Effect of Processing on Carbohydrate Fractionation and Influence of Grain Starch on Protein Utilization in Albino Rats

Jamil¹,

Bashir²,

Yaqoob³

1999

Pakistan J. of Biological Sciences

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“…Numerous studies have demonstrated that cereal grains contain variable numbers of proteins with characteristics of digestive enzyme inhibitors of mammals, insects, and bacteria (1)(2)(3)(4)(5)(6)(7). These proteins for many years were recognized only as undesirable, anti-nutritional substances: they decrease the availability of nutritional components (6)(7)(8)(9)(10)(11) and moreover are listed among protein fractions causing food allergies ( 12,13 ) .…”

mentioning

confidence: 99%

“…These proteins for many years were recognized only as undesirable, anti-nutritional substances: they decrease the availability of nutritional components (6)(7)(8)(9)(10)(11) and moreover are listed among protein fractions causing food allergies ( 12,13 ) . However, in recent years, more and more studies have demonstrated that these proteins can be utilized as components of therapeutic and health-related products under some conditions ( 8 , 14, 15 ).…”

mentioning

confidence: 99%

Digestive Enzyme Inhibitors from Grains as Potential Components of Nutraceuticals

Piasecka‐Kwiatkowska

Warchalewski

Zielińska‐Dawidziak

et al. 2012

J Nutr Sci Vitaminol

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Summary Inhibitor activity against digestive enzymes, such as ␣ -amylase from human saliva and porcine pancreas and trypsin from bovine pancreas, of three cereal grains species were studied as potential components of nutraceuticals strengthening diabetes and obesity treatment. Significant differences were demonstrated: the highest antitryptic activity was found in the grain of the rye varieties studied, whereas the grain of the wheat varieties had significantly higher ability to inhibit ␣ -amylases from human saliva and porcine pancreas. Additionally, seeds of Puma, one of the studied wheat varieties, demonstrated especially low antitryptic activity. Such a beneficial arrangement of inhibitors, i.e. high level of inhibitors of ␣ -amylase from human saliva and porcine pancreas and simultaneously low level of trypsin inhibitors from bovine pancreas, indicate the possibility of the application of seeds with such properties to the preparation of nutraceuticals for people with obesity or suffering from diabetes.

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“…The family of wheat a-amylase inhibitors (a-AIs) comprises numerous protein members that share up to 98% sequence homology [1,2]. These proteins can inhibit endogenous and hexogenous a-amylase, an enzyme that plays an important role in the carbohydrate metabolism of many autotrophic and heterotrophic organisms [3,4].…”

Section: Introductionmentioning

confidence: 99%

Full‐fledged proteomic analysis of bioactive wheat amylase inhibitors by a 3‐D analytical technique: Identification of new heterodimeric aggregation states

et al. 2007

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Full-fledged proteomic analysis of bioactive wheat amylase inhibitors by a 3-D analytical technique: Identification of new heterodimeric aggregation statesWheat proteinaceous a-amylase inhibitors (a-AIs) are increasingly investigated for their agronomical role as natural defence molecules of plants against the attack of insects and pests, but also for their effects on human health. The wheat genomes code for several bioactive a-AIs that share sequence homology, but differ in their specificity against a-amylases from different species and for their aggregation states. Wheat a-AIs are traditionally classified as belonging to the three classes of tetrameric, homodimeric and monomeric forms, each class being constituted by a number of polypeptides that display different electrophoretic mobilities. Here we describe a proteomic approach for the identification of bioactive a-AIs from wheat and, in particular, a 3-D technique that allows to best identify and characterize the dimeric fraction. The technique takes advantage of the thermal resistance of a-AIs (resistant to T . 707C) and consists in the separation of protein mixtures by 2-D polyacrylamide/starch electrophoresis under nondissociating PAGE (ND-PAGE, first dimension) and dissociating (urea-PAGE or U-PAGE second dimension) conditions, followed by in-gel spontaneous reaggregation of protein complexes and identification of the a-amylase inhibitory activity (antizymogram, third dimension) using enzymes from human salivary glands and from the larvae of Tenebrio molitor coleopter (yellow mealworm). Dimeric a-AIs from Triticum aestivum (bread wheat) were observed to exist as heterodimers. The formation of heterodimeric complexes was also confirmed by in vitro reaggregation assays carried out on RP-HPLC purified wheat dimeric a-AIs, and their bioactivity assayed by antizymogram analysis. The present 3-D analytical technique can be exploited for fast, full-fledged identification and characterization of wheat a-AIs.

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α-amylase inhibitors from wheat: Amino acid sequences and patterns of inhibition of insect and human α-amylases

Cited by 99 publications

References 24 publications

Studies on Vigna mango L. - Effect of Processing on Carbohydrate Fractionation and Influence of Grain Starch on Protein Utilization in Albino Rats

Studies on Vigna mango L. - Effect of Processing on Carbohydrate Fractionation and Influence of Grain Starch on Protein Utilization in Albino Rats

Digestive Enzyme Inhibitors from Grains as Potential Components of Nutraceuticals

Full‐fledged proteomic analysis of bioactive wheat amylase inhibitors by a 3‐D analytical technique: Identification of new heterodimeric aggregation states

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