Proteolytic Action of Pepsin on Glutenin

Oka, Shinji; Babel, F.J.; Draudt, H. N.

doi:10.1111/j.1365-2621.1965.tb00291.x

Cited by 10 publications

(7 citation statements)

References 8 publications

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“…However, free amino acid nitrogen was not detected until 12 h of hydrolysis, when free phenylalanine, leucine, valine, and tyrosine were present. Proteolysis of glutenin by pepsin was shown by Oka et al (1965) to rapidly decrease the viscosity of the dispersion and increase the water-soluble fraction. These workers suggested that these early changes were results of cleavage of a few F(O.Ol)l,ll = 9.65**; F(0.05)1,11 = lated boundary condition; a response of 1.00 was arbitrarily assigned t o force the factor back inside the boundary by a contraction.…”

Section: Resultsmentioning

confidence: 98%

Covalent attachment of lysine to wheat gluten for nutritional improvement

Li‐Chan¹,

Helbig²,

Holbek³

et al. 1979

J. Agric. Food Chem.

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The lysine content of wheat gluten was increased up to fourfold after reaction of pepsin-hydrolyzed wheat gluten with N'-benzylidenelysine in the presence of l-ethyl-3-(3-dimethylaminopropyl)carbodiimide. Although partially acid-hydrolyzed gluten reacted with L-lysine hydrochloride, thus increasing the lysine content up to 20-fold, the available lysine determined by the dinitrobenzenesulfonate method and the liberated lysine by the pepsin pancreatin digestion method were low, 48 and 41 % , respectively. This result suggests formation of y-a, y e , and a-e isopeptide bonds. When a reversibly €-amino protected lysine, N'-benzylidenelysine, was used for binding, the available lysine content increased to 91 % . However, the liberated lysine value stayed the same, suggesting the possibility of y-a bond formation. When pepsin hydrolysis instead of acid was used for solubilization of gluten, the liberated lysine value was improved to 65% compared to 31 and 45% for egg and casein, respectively. The bound lysine residues in the pepsin-hydrolyzed gluten were readily digestible and available.

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Section: Resultsmentioning

confidence: 98%

Covalent attachment of lysine to wheat gluten for nutritional improvement

Li‐Chan¹,

Helbig²,

Holbek³

et al. 1979

J. Agric. Food Chem.

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“…Small amounts of proteases can have large effects on gluten physical properties. Oka et al. (1965) demonstrated that breakage of a few peptide bonds resulted in a rapid decrease in viscosity of glutenin dispersion.…”

Section: Introductionmentioning

confidence: 99%

“…Small amounts of proteases can have large effects on gluten physical properties. Oka et al (1965) demonstrated that breakage of a few peptide bonds resulted in a rapid decrease in viscosity of glutenin dispersion. Also, Redman (1971) reported evidence to support the hypothesis that gluten softening is the direct result of peptide bond scission catalyzed by proteases.…”

Section: Introductionmentioning

confidence: 99%

Study on Interaction Among Extrusion‐cooking Process Variables and Enzyme Activity: Evaluation of Extrudate Structure

Pilli

Legrand

Derossi

et al. 2010

J Food Process Engineering

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A blend of wheat flour (moisture content 11.61%) and different amounts of two commercial enzymes like GRINDAMYL (GA) amylase 1000 (0–0.1 g/kg) and GA protease 41 (0–1.0 g/kg) were extruded through a co‐rotating twin‐screw extruder. The effects of barrel temperature (60–120C), dough moisture (20–36%), screw speed (100–400 rpm) and different amounts of enzymes on structure of extrudates (porosity and break strength) were studied using response surface methodology. Results showed that the highest value of porosity (62.47% ± 4.07) was obtained at the highest value of barrel temperature (120C) and at the largest amounts of GA protease 41 (1.0 g/kg) or GA amylase 1000 (0.1 g/kg). However, the simultaneous addition of large amounts of both enzymes caused a negative effect on expansion degree (porosity < 30%). Large amounts of moisture dough and GA amylase 1000 resulted in a high value of break strength (25.7 N/mm2) and in stiff‐textured extrudates. PRACTICAL APPLICATIONS This research could provide some information about the effects of and the interactions between extrusion parameters and enzyme activities, which are commonly used to produce bakery products, in order to improve the texture of extrudates processed at low barrel temperatures, i.e., 60C, for example, extrudates with thermolabile components like vitamins or extrudates with high lipid fraction like breakfast cereals, pet food, etc.

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“…Small amounts of proteases can have a large effect on gluten physical properties. Oka et al. (1965) demonstrated that breakage of a few peptide bonds resulted in a rapid decrease in viscosity of glutenin dispersion.…”

Section: Introductionmentioning

confidence: 99%

Improving Fatty Extrudate Structure With Amylase and Protease

Pilli

Severini

Carbone

et al. 2004

Journal of Food Biochemistry

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The extrusion of fatty flour at temperatures less than 100C on the one hand favors less leakage of oil from plant and products, but on the other hand reduces the degree of expansion unless suitable technological coadjuvants are used.Enzymes are generally used in the preparation of bread to mellow gluten and to soften texture. At the moment, there is little information about the use of enzymes to improve the texture of extruded products.The effect of two commercially available enzymes (GRINDAMYL Amylase 1000 and GRINDAMYL Protease 41) on the texture of products obtained from wheat and almond flours extruded at low temperature (54C) was studied.GRINDAMYL Protease 41 was found to affect the rheological characteristics of dough by rapid decreasing the consistency during farinographic analyses and by improving the structure of extrudates with a high lipid content (reduced breaking strength, high% porosity and high water solubility index).

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Proteolytic Action of Pepsin on Glutenin

Cited by 10 publications

References 8 publications

Covalent attachment of lysine to wheat gluten for nutritional improvement

Covalent attachment of lysine to wheat gluten for nutritional improvement

Study on Interaction Among Extrusion‐cooking Process Variables and Enzyme Activity: Evaluation of Extrudate Structure

Improving Fatty Extrudate Structure With Amylase and Protease

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