Interactions of Protein and Starch Studied Through Amyloglucosidase Action

Guerrieri, N.; Eynard, L.; Lavelli, Vera; Cerletti, Paolo

doi:10.1094/cchem.1997.74.6.846

Cited by 37 publications

(30 citation statements)

References 9 publications

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“…In conclusion, the study conducted in this work supports our previous hypothesis of an interaction between dextrin and gliadins (9). Moreover, in agreement with Grant et al (39) we found that, despite their low solubility in water, gliadins have hydrophilic character as evidenced by hydrogen-bond formation with water molecules and dextrin.…”

Section: Discussionsupporting

confidence: 93%

ATR-FT/IR Study on the Interactions between Gliadins and Dextrin and Their Effects on Protein Secondary Structure

Secundo

Guerrieri

2005

J. Agric. Food Chem.

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124

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The effects of heat treatment and dextrin addition on the secondary structure of gliadins were investigated by means of attenuated total reflection Fourier transform infrared spectroscopy (ATR-FT/IR). Gliadins and gliadin/dextrin mixtures (before and after thermal treatment) were prepared as a dried protein film on the ATR-FT/IR zinc selenide cell plate and equilibrated at a water activity (a(w)) of 0.06. The results show that gliadins undergo conformational changes upon thermal treatment both in the absence and in the presence of dextrin. In particular, in the thermally treated gliadins, the decrease of the band at around 1651 cm(-)(1) and the increase of the bands at around 1628 and 1690 cm(-)(1) suggest a loss of alpha-helix structure and a higher content of protein aggregates. The same trend was observed in the presence of dextrin. Concerning the interactions between gliadins and dextrin, gliadin/dextrin mixtures show variations in the amide I region compared to native gliadins (e.g., an increase of the band at 1645 cm(-)(1) and the absence of the band at around 1668 cm(-)(1)) that might be due to hydrogen bond formation between gliadins and dextrin. It was also found that the spectrum of gliadin/dextrin mixtures was less affected by the hydration state than that of native gliadins, as observed from the differential spectra obtained by subtraction of the spectrum obtained at a(w) = 0.06 (driest condition tested) from the spectrum of the sample equilibrated at a(w) = 0.84. This could be due to the fact that C=O and N-H groups of gliadins are engaged to form hydrogen bonds with the hydroxyl groups of dextrin, and so they are not perturbed by the presence of water molecules. Finally, water activity effects on the secondary structure of gliadins are also discussed.

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Section: Discussionsupporting

confidence: 93%

ATR-FT/IR Study on the Interactions between Gliadins and Dextrin and Their Effects on Protein Secondary Structure

Secundo

Guerrieri

2005

J. Agric. Food Chem.

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124

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“…It has been suggested that the interaction between the starch granules and the surrounding protein matrix may reduce the accessibility of amylolytic enzymes to starch granules in hard wheat (Guerrieri et al, 1997;Peron et al, 2006). It has been suggested that the interaction between the starch granules and the surrounding protein matrix may reduce the accessibility of amylolytic enzymes to starch granules in hard wheat (Guerrieri et al, 1997;Peron et al, 2006).…”

Section: Feed Particle Size and Exogenous Enzymementioning

confidence: 99%

Influence of feed processing on the efficacy of exogenous enzymes in broiler diets

Amerah¹,

Gilbert²,

Simmins³

et al. 2011

World's Poultry Science Journal

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The use of commercial exogenous enzymes in poultry diets is now a common practice. Broilers are predominantly fed pelleted diets; of the various unit operations in the production of pellets, grinding and conditioning are the components that can influence the efficacy of exogenous enzymes. The aim of this paper was to review the feed processing factors that influence the efficacy of exogenous enzymes in broiler diets. Recent studies have shown that the efficacy of exogenous enzymes is influenced by the degree of grinding. Available data suggest that enzyme responses on intestinal viscosity are more pronounced in feeds subjected to high conditioning temperatures. The issue of enzyme stability during conditioning and pelleting therefore becomes relevant and new enzyme technologies are being developed to overcome the high thermal processing issues. However, the effects of steam conditioning practices on enzyme stability have received less attention and need to be explored in future studies.

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“…The polyacrylamide gel was prepared with a monomer mixture of 8.4YoT and 4.80' oC in 25 mM sodium lactate adjusted to pH 3.1 with NaOH. Electrophoresis was performed as described in Guerrieri et al [29]. The proteins in the gel were fixed for 20 rnin with 100 mL of 12% w/v trichloroacetic acid and stained overnight with 100 mL of 12% w/v trichloroacetic acid plus 10 mL of 5 mg/mL Coomassie Brilliant Blue G-250.…”

Section: Protein Extractionmentioning

confidence: 99%

Wheat cultivar discrimination by capillary electrophoresis of gliadins in isoelectric buffers

et al. 1998

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A modified method is reported for screening of wheat cultivars: capillary zone electrophoresis of gliadins in isoelectric buffers. Previously published procedures recommended a 100 mM phosphate buffer, supplemented with 0.05% hydroxypropylmethylcellulose and 20% acetonitrile, in uncoated capillaries. Due to the very high conductivity of such a buffer (4.7 mmhos at 25 degrees C) high speed separations (10-12 min analysis time at 800 V/cm) could only be elicited in 20 microm internal diameter (ID) capillaries, at the expense of sensitivity. In the present report, we optimized the background electrolyte as follows: 40 mM aspartic acid (pH=pI=2.77) in the presence of 7 M urea and 0.5% short-chain hydroxyethylcellulose (Mn 27000 Da; apparent pH 3.9 in 7 M urea). As an alternative recipe, the same isoelectric buffer can be supplemented with a mixed organic solvent composed of 4 M urea and 20% acetonitrile (apparent pH 3.66). Due to the much lower conductivity (0.7 mmhos), separations can be carried out at 1000 V/cm in only 10 min, but in larger bore capillaries (50 microm ID), ensuring a five-times higher sensitivity. The gliadin patterns thus obtained are species-specific and allow easy identification of all cultivars tested of both durum and bread wheat. No adsorption of proteins to the silica wall seems to occur and high reproducibility in peak areas and transit times is obtained.

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Interactions of Protein and Starch Studied Through Amyloglucosidase Action

Cited by 37 publications

References 9 publications

ATR-FT/IR Study on the Interactions between Gliadins and Dextrin and Their Effects on Protein Secondary Structure

ATR-FT/IR Study on the Interactions between Gliadins and Dextrin and Their Effects on Protein Secondary Structure

Influence of feed processing on the efficacy of exogenous enzymes in broiler diets

Wheat cultivar discrimination by capillary electrophoresis of gliadins in isoelectric buffers

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