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Abstract  

The study deals with the effect of chemical and physical modifications on thermal properties and solubility properties of films based on amaranth flour starch–protein hydrolysate. Biodegradable and edible films were prepared by casting a 25% (w/w) solution of hydrolysate containing 20% glycerol and various additions of dialdehyde starch (0, 1 and 5%). After thermal exposure of films at 65 and 95 °C (for 6 and 48 h), thermal properties of films were studied employing differential scanning calorimetry and thermogravimetric analysis. Film solubility tests were performed in an aqueous environment at 25 °C. Chemical and physical modifications of films markedly affect their thermal properties and solubility.

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Adler-Nissen, J. (1979): Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. J. agric. Fd Chem. , 27 , 1256-1260. Determination of

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Acta Biologica Hungarica
Authors: Huan Zhang, Pan Wang, Ai-Jun Zhang, Xuan Li, Ji-Hong Zhang, Qi-Lian Qin, and Yi-Jun Wu

. Food Chem. 50 , 1619 - 1624 . 6. Quian , Z. , Jung , W. , Kim , S. ( 2008 ) Free radical scavenging activity of a novel antioxidative peptide purified from hydrolysate

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dietétique Clemente, A. (2000): Enzymatic hydrolysates on human nutrition. Trends Fd Sci. Technol., 11 , 254-262. Enzymatic hydrolysates on human nutrition

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groundnut protein hydrolysate and peptide fractions against angiotensin-converting enzymes, renin and free radicals . J. Sci. Food Agr. , 97 , 2834 – 2841 . A soodeh , A. , H aghighi

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Acta Alimentaria
Authors: Z. Jrad, H. El Hatmi, I. Adt, T. Khorchani, P. Degraeve, and N. Oulahal

The aim of this study was to evaluate the antimicrobial activity of camel caseins and their hydrolysates by gastrointestinal proteolytic enzymes against 3 Gram-positive and 2 Gram-negative bacterial strains. Camel caseins (CN) were hydrolysed by successive action of pepsin and pancreatin. Hydrolysis of CN was checked by electrophoresis and gel filtration chromatography (GFC). Both techniques showed that CN was hydrolysed into peptides. Among the tested bacteria, a decrease of 19.3%±0.02 of E. coli XL1 blue cells growth was observed in the presence of undigested camel casein at a concentration of 20 mg ml−1. After successive hydrolyses by pepsin and pancreatin, camel milk casein hydrolysates still exhibited anti-bacterial activity against E. coli XL1 blue strain (19.73±0.01% growth inhibition under the same conditions). Gram-positive strain growth was not affected by intact camel CN, while, at the same concentration (20 mg ml–1), their hydrolysates slightly inhibited the growth of these bacteria. This suggests that antibacterial peptidic fragments of caseins were generated by pepsin and pancreatin.

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Abstract  

Processing hydrogels of collagen hydrolysate (H) cross-linked with dialdehyde starch (DAS) by dipping or casting into biodegradable materials for various applications, is complicated by their marked tendency to aging. One-hour action by temperatures at 60–90 °C reduces sorbed water content in hydrogels by approx. 12%; dependence of the extent of this reduction on temperature (within the mentioned range) was not detected. Effect of thermal action on duration of their disintegration in an aqueous medium and on its pH (within limits 4.8–7.4) was not found either, neither on their gel–sol transition temperature. This supports the view that aging is caused by time-dependent increasing network density of inter-chain hydrogen cross-links. The given temperature interval is satisfactory for processing hydrogels through technologies currently used in processing synthetic plastics (compression molding, injection molding).

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Abstract  

Hydrolysates from chromed leather waste obtained in powdered form on an industrial scale by using biotechnical methods were analysed by TG an DSC techniques. Besides about 9% (mass/mass) of moisture, around 1% (mass/mass) of cyclohexylamine was found in the pulverized hydrolysates. Calorimetric measurement of the reaction heats of the reactions of the hydrolysates with commercially available aldehydes indicates that their reactivity decreases in the sequenceglutardialdehyde>>methylglyoxal≈acetaldehyde>>glyoxal>formaldehyde.

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Abstract  

Condensation of dimethylol-urea (DMU) mixed with urea (U) and collagen hydrolysate (H), obtained through enzymatic hydrolysis of chrome-tanned leather waste, without added acid curing agents in the solid phase was studied through DSC and TG techniques in a temperature interval up to 220°C. Among both techniques TG proved be more useful.While the DMU+U mix produced methylene-oxide (-CH2-O-CH2-) and methylene (-CH2-) bridges at a ratio of approx. 1:1, urea substituted for collagen hydrolysate increased the proportion of more stable methylene bridges to methylene-oxide bridges to a ratio of approx. 2:1. Methylene-oxide bridges are considered to be the main potential sources of formaldehyde emissions from cured urea-formaldehyde type adhesives, and thus the use of collagen hydrolysate in preparation of urea-formaldehyde adhesive types is a suitable way how to make such adhesives more environmental friendly.

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Abstract  

The process of cross-linking of collagen phosphoric acid hydrolysates (CH) with cyanuric chloride (CY) was studied by the increase in the denaturation temperature using differential scanning calorimetry (DSC). This measurement gave indications concerning the efficiency of the treatment, i.e., the extent of cross-linking of the collagen hydrolysates. The optimal conditions for cross-linking were determined: CH/CY in a ratio 1:1, reaction time 1 h at temperature 50 °C. At these conditions cross-linked structural units with higher thermal stability were formed.

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