Veränderungen der funktionellen Eigenschaften von <i>Vicia‐faba</i>‐Proteinisolaten durch partielle enzymatische Hydrolyse

Behnké, U.; Schultz, M.; Ruttloff, H.; Schmandke, H.

doi:10.1002/food.19820260313

Cited by 9 publications

(5 citation statements)

References 19 publications

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“…These amino acids are linked together by peptide bonds to form the high molecular weight proteins. Some of these bonded amino Some of these degradation products contribute useful functional properties, such as physicofunctionality (1)(2)(3)(4)(5)(6), dietetic or nutritive properties (7)(8)(9)(10)(11)(12), and flavor sensations (13)(14)(15)(16)(17). Meat flavor is a product of protein degradation and the greatest part of industrially produced protein hydrolysates is used to provide meat flavorants.…”

Section: Introductionmentioning

confidence: 99%

Protein hydrolysis—the key to meat flavoring systems

Lieske

Konrad

1994

Food Reviews International

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The flavors produced by stewing, broiling, or roasting make meat one of the most popular items in the human diet. No "key" compounds are responsible for meat flavors. However, protein degradation appears essential to the development of meat flavor precursors whose interactions are responsible for characteristic meat flavors. This review examines simulated meat flavor systems based on the protein degradation products produced by acid hydrolysis using strong mineral acids, yeast autolysis, and enzyme degradation of natural meat proteins by pure proteinases. In addition, the contributions to meat flavor made by heating protein hydrolysates in the presence of sugars and organic sulfur compounds are reviewed. This paper also describes the work in applied meat flavor research carried out in the former East Germany.

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Section: Introductionmentioning

confidence: 99%

Protein hydrolysis—the key to meat flavoring systems

Lieske

Konrad

1994

Food Reviews International

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“…Special investigations were performed by several laboratories on the effect of proteolytic degradation on the emulsifying properties of proteins from animal and vegetable origin such as milk [2, 3, 41, soybeans [5, 61, wheat gluten [7], oats [8] and faba beans [9]. In previous papers the effect of limited tryptic breakdown of faba bean legumin to the high molecular mass intermediate product "1egumin-T" on the surface funtional properties were studied [ 101.…”

Section: Introductionmentioning

confidence: 99%

Changes in interfacial properties of legumin from faba beans (Vicia faba I.) by tryptic hydrolysis

Krause

Schwenke

1995

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SummaryChanges of the surfxe tension at a planar interface and of the emulsifying properties of tryptically digested legumin from faba beans (enzyme/substrate ratio = 1/40) were studied in terms of time of hydrolysis (0-48 h). Simultaneously, molecular changes of legumin were studied by determination of liberated amino groups, RP-HPLC. and SDS-PAGE analysis.While the surface tension continuously decreases with increasing amount of liberated amino groups, improved emulsion properties, i.e. decreasing droplet size and increasing coalescence as well as creaming stability, were only observed during the first 240 min of hydrolysis, where incredse in the content of free amino groups amounted to 18-24 free amino groups per protein subunit. The surface tension during the diffusion-controlled phase reached the lowest value after a hydrolysis time of 24 h which corresponds to an increase of 44-50 free amino groups per protein subunit. Additionally, the results support the view that the interfacial adsorption at quiet interfaces and during emulsion formation are governed by different transport mechanisms. ZusammenfassungVeranderungen des Adsorptionsverhaltens des Legumins der Ackerbohne (Vicia $aha L.) an der planaren Luft/Wasser-Grenzflache sowie der Emulgieraktivitat wurden in Abhangigkeit von der Dauer der tryptischen Hydrolyse (0-48 h) bei einem Enzym/Substratverhlltnis von 1/40 untersucht. Die Bestimmung der Zahl freier Aminogruppen (NH,) sowie RP-HPLC und SDS-PAGE-Untersuchungen gaben AufschluB uber strukturelle Veranderungen des Legumins wahrend der Hydrolyse. Die Oberflachenspannung nimmt nahezu linear mit steigender Zahl freigesetzter Aminogruppen a b und erreicht den niedrigsten Wert nach einer Hydrolysezeit von 24 h (44 -50 Aminogruppen pro Untereinheit). Verbesserungen der Emulsionseigenschaften, wie abnehmende TropfchengroBe oder erhohte Koaleszenz-und Aufrahmstabilitlt, sind nur wiihrend der ersten 240 min der Hydrolyse zu verzeichnen. Die Zahl zusltzlicher freier Aminogruppen lag zwischen 18 und 24 Aminogruppen pro Leguminuntereinheit. Die Ergebnisse stiitzen die These, dal3 unterschiedliche Transportmechanismen und somit verschiedene Fraktionen des hydrolysierten Leguminmolekuls die diffusionskontrollierte Phase der Adsorption und die Homogenisierung bestimmen.

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“…After adding of glucoamylase (2.25 AGU/g of starch), hydrolyzate is saccharified for 9 h at 60 "C and enzyme is inactivated for 10 min at 90 "C. Further steps of proteolysis are the same as in procedure 1. (TNBA) [8] or by pH stat titration [I].…”

Section: Gradual Amylolytic-proteolytic Hydrolysis Using Glucoamylasementioning

confidence: 99%

“…Such hydrolyzates are e.g. known of soy beans [l-41, wheat [5-71, field beans [8], rape [9], and others. Their special functional properties (e.g.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic hydrolysis of maize protein

Behnké

Jurišová

Belajová

et al. 1989

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Maize proteins are hydrolyzed by proteinases to a much less extent than soy, wheat, meat, fish or milk proteins. An industrial use of this process has not become known yet. Own investigations with technical maize gluten deal with the comparison of the enzymatic hydrolysis of maize and wheat gluten and investigation of some functional properties of the hydrolyzates, the comparison of different proteinases, the influence of different kinds of pretreatment (HCI, a-amylase, heating) on the enzymatic proteolysis of the starch containing gluten samples and the estimation of molecular weight distribution of maix gluten hydrolyzates.From the results it is obvious that the solubilities of maize gluten hydrolyzates are significantly less than those from wheat gluten with comparable degrees of hydrolysis. Special investigations on the solubilities and the distribution of molecular weights reveal that preferably small peptides besides not or only little attacked proteins are found as hydrolysis products. Despite of using selected pretreatment methods the extent of hydrolysis can be increased only partly. 24a*

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Veränderungen der funktionellen Eigenschaften von Vicia‐faba‐Proteinisolaten durch partielle enzymatische Hydrolyse

Cited by 9 publications

References 19 publications

Protein hydrolysis—the key to meat flavoring systems

Protein hydrolysis—the key to meat flavoring systems

Changes in interfacial properties of legumin from faba beans (Vicia faba I.) by tryptic hydrolysis

Enzymatic hydrolysis of maize protein

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