Literature DB >> 1138913

Inhibition of amylases from different origins by albumins from the wheat kernel.

V Silano, M Furia, L Gianfreda, A Macri, R Palescandolo, A Rab, V Scardi, E Stella, F Valfre.   

Abstract

The amylase activity of water extracts from 18 insect species, from 23 marine species and from 17 different species of birds and mammals was determined quantitatively. The inhibition of amylase in these extracts by three albumin fractions from the mature wheat kernel, which had been separated according to their molecular weights (60 000, 24 000 and 12 500 D), was determined as well. The inhibition activity of the three albumin fractions toward amylases extracted from a number of cereal species or from immature and germinating wheat kernel was also tested. The extracts from insects that are destructive of wheat grain and stored wheat products showed much higher amylase activities as compared to the other insect species that do not attack wheat and wheat products. On the basis of the effectiveness with which the three albumin fractions inhibit their activities, the amylase preparations tested were divided into susceptible, partially susceptible and resistent. Susceptible amylases, inhibited by any of the three albumin fractions, were found mainly in insects that attack wheat and in marine species. Partially susceptible amylases, inhibited by only one or two of the three albumin fractions, were present in a few avain and mammalian species including man. Resistent amylases were largely distributed in cereal, avian and mammalian species as well as in insect species that do not usually attack wheat grain or wheat flour products. At no stage of development, wheat alpha-amylase was inhibited by the albumin fractions from the mature kernel. The 12 500 dalton albumin fraction was the most effective in inhibiting insect amylases, but it was inactive toward avian and mammalian amylases. The 24 000 dalton albumin fraction was the most effective in inhibiting amylases from marine avian and mammalian species and inhibited as much as 33 amylases over 66 different amylases tested. It is suggested that protein inhibitors of amylase contributed to natural selection of polyploid wheats by giving some insect resistence to such wheats, even though some insect species were able to overcome this biochemical defense toa large degree by producing higher amylase activities.

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Year:  1975        PMID: 1138913     DOI: 10.1016/0005-2744(75)90163-1

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  10 in total

1.  Modulation of key metabolic enzyme of Labeo rohita (Hamilton) juvenile: effect of dietary starch type, protein level and exogenous alpha-amylase in the diet.

Authors:  Shivendra Kumar; N P Sahu; A K Pal; Vidya Sagar; Amit Kumar Sinha; Kartik Baruah
Journal:  Fish Physiol Biochem       Date:  2008-04-04       Impact factor: 2.794

2.  Structural studies of wheat monomeric and dimeric protein inhibitors of alpha-amylase.

Authors:  T Petrucci; G Sannia; R Parlamenti; V Silano
Journal:  Biochem J       Date:  1978-07-01       Impact factor: 3.857

3.  The phylogenesis of protein α-amylase inhibitors from wheat seed and the speciation of polyploid wheats.

Authors:  L Vittozzi; V Silano
Journal:  Theor Appl Genet       Date:  1976-11       Impact factor: 5.699

4.  Purification and properties of alpha-amylase from chicken (Gallus gallus L.) pancreas.

Authors:  V Buonocore; R Deponte; F Gramenzi; T Petrucci; E Poerio; V Silano
Journal:  Mol Cell Biochem       Date:  1977-08-19       Impact factor: 3.396

5.  Protective mechanism of the Mexican bean weevil against high levels of alpha-amylase inhibitor in the common bean.

Authors:  M Ishimoto; M J Chrispeels
Journal:  Plant Physiol       Date:  1996-06       Impact factor: 8.340

6.  The amylase gene-enzyme system of chickens. II. Biochemical characterization of allozymes.

Authors:  R A Gapusan; D G Yardley; B L Hughes
Journal:  Biochem Genet       Date:  1990-12       Impact factor: 1.890

7.  Interaction of wheat monomeric and dimeric protein inhibitors with alpha-amylase from yellow mealworm (Tenebrio molitor L. larva).

Authors:  V Buonocore; F Gramenzi; W Pace; T Petrucci; E Poerio; V Silano
Journal:  Biochem J       Date:  1980-06-01       Impact factor: 3.857

8.  The purification of a novel amylase from Bacillus subtilis and its inhibition by wheat proteins.

Authors:  A R Orlando; P Ade; D Di Maggio; C Fanelli; L Vittozzi
Journal:  Biochem J       Date:  1983-02-01       Impact factor: 3.857

9.  Triticum aestivum puroindolines, two basic cystine-rich seed proteins: cDNA sequence analysis and developmental gene expression.

Authors:  M F Gautier; M E Aleman; A Guirao; D Marion; P Joudrier
Journal:  Plant Mol Biol       Date:  1994-04       Impact factor: 4.076

10.  Genes encoding α-amylase inhibitors are located in the short arms of chromosomes 3B, 3D and 6D of wheat (Triticum aestivum L.).

Authors:  R Sanchez-Monge; D Barber; E Mendez; F García-Olmedo; G Salcedo
Journal:  Theor Appl Genet       Date:  1986-04       Impact factor: 5.699

  10 in total

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