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Abstract  

Hydrogels of collagen hydrolysate (H) of mean M w 15–30 kDa obtained from waste collagen from meat casings manufacture, cross-linked with 15% (based on H) polymeric dialdehyde starch (DAS), have a marked tendency to ageing, which shows in hydrogel gradually increasing rigidity and decreasing thermo-reversibility. Methods of thermal analysis (DSC, TG) proved that ageing of hydrogels is not related with a non-equilibrium state of the cross-linking reaction but is rather given by increasing density of inter-chain hydrogen bonds between polypeptide segments of H. Plasticizing effect of DAS on H is not too pronounced but the difference between glass transition temperature of dry xerogel T g = 189.5±2.5°C and temperature of starting degradation (DAS component) 241.4±12.7°C offers certain space for processing these xerogels into biodegradable (edible) packaging material by usual plastics technologies. Films obtained from the reaction mixture by casting and drying at room temperature after thermal processing (105°C for 4 h) dissolve at room temperature only after 350 h. This effect can be employed for time-controlled releasing of active substances from such biodegradable (edible) packages.

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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  

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  

Gels of collagen hydrolysate (H) crosslinked with dialdehyde starch (DAS) are marked by a strong tendency to aging, which means a certain problem during their processing into biodegradable packaging materials. Applying casting technology and drying these materials by heating air-dry films and foils for a limited time (1–4 h) at 105 °C may eliminate the aging problem. Solubility of heat-treated films in an aqueous environment remains preserved, but depending on how long this temperature acts and on the DAS content in the film, time of film disintegration prolongs from 1–1.5 h to 1300 h (≈54 days). It is probably caused by the functional groups initially blocked by sorbed water, which get released to produce hydrogen inter-chain crosslinks. The decrease in glass transition temperature (T g) of such films varies with content of water sorbed in films in an interval of 90.2–189 °C.

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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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Abstract  

Differential scanning calorimetry was employed to investigate the reaction of diglycidyl ethers of bisphenol A (DGEBA) of mean molecular mass 348–480 Da, with collagen hydrolysate of chrome-tanned leather waste in a solvent-free environment. The reaction leads to biodegradable polymers that might facilitate recycling of plastic parts in products of the automotive and/or aeronautics industry provided with protective films on this basis. The reaction proceeds in a temperature interval of 205–220°C, at temperatures approx. 30–40°C below temperature of thermal degradation of collagen hydrolysate. The found value of reaction enthalpy, 519.19 J g−1 (= 101.24 kJ mol−1 of epoxide groups) corresponds with currently found enthalpy values of the reaction of oxirane ring with amino groups. Reaction heat depends on the composition of reaction mixture (or on mass fraction of diglycidyl ethers in the reaction mixture); proving the dependence of kinetic parameters of the reaction (Arrhenius pre-exponential factor A (min−1) and activation energy E a (kJ mol−1)) did not succeed. Obtained values of kinetic parameters are on a level corresponding to the assumption that reaction kinetics is determined by diffusion.

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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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-I converting enzyme inhibitory peptides from sea cucumber collagen hydrolysates . J. Aquat. Food Prod. T. , 20 , 222 – 232 . L ombard , J.H. & D elange , D.J. ( 1965 ): The chemical

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, J , Mládek , M , Kolomazník , K . Curing adhesives of urea-formaldehyde type with collagen hydrolysates of chrome-tanned leather waste . J Therm Anal Calorim . 2004 ; 75 : 205 – 219 . 10.1023/B:JTAN.0000017343.45997.6e

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-treated biodegradable films and foils of collagen hydrolysate crosslinked with dialdehyde starch . J Therm Anal Calorim . 2010 ; 102 : 37 – 42 . 10.1007/s10973-009-0525-2 . 10. Weadock , KS , Miller

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