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Background. Meat products belong to products particularly at risk of fat oxidation processes. One of the methods to prevent disadvantageous oxidative changes of lipids in food is the application of antioxidants. Material and methods. The experimental material consisted of fine - ground model sausages. Produced processed meats differed in terms of the presence and amount of acid and enzymatic soy hydrolysates (0.3% and 0.7%). The reference sample comprised processed meat product with no hydrolysate added. Model processed meat products were stored at 4°C for 29 days. The analyses included changes in peroxide value, changes in cholesterol and its oxidation products. Results. It was found that changes of peroxide value, 7α-OHC, 7β-OHC, α-epoxy-C, β-epoxy-C, 20α-OHC, 25-OHC and total oxisterols were statistically significantly af-fected, apart from storage time, also by the type and level of applied hydrolysates. The addition of enzymatic and acid hydrolysates to batter of experimental sausages effectively inhibited the process of fat oxidation. Conclusions. In samples with enzymatic hydrolysate an approx. 20% loss of initial cholesterol content was recorded. In contrast, in the other samples this loss amounted to approx. 10%. The process of cholesterol metabolism in tested processed meat products was affected by their storage time and the type of added hydrolysate. It was observed that the highest dynamics of cholesterol metabolism occurred in a sample with no hydrolysate added. The level of total oxisterols in the sample with no addition of hydrolysate was over two times higher than in samples with an addition of hydrolysate.
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The antioxidant capacity as free radicals of 1,1 diphenyl-2-picryhydrazyl (DPPH) scavenger of egg white protein hydrolysate was investigated. Egg white protein precipitate obtained as a by-product in cystatin and lysozyme isolation was hydrolysed with bovine trypsin and then separated by means of RP-HPLC. Of ten fractions collected only no. 2 (0.195 μmol Trolox /mg) and no. 5 (0.186 μmol Trolox /mg) displayed a considerable free radicalscavenging capacity. The rechromatography of these fractions yielded four products of raised antioxidant activity: no. 2E (obtained from fraction no. 2) and no. 5E, 5F, 5H (obtained from fraction no. 5) which amounted to 0.482 μmol Trolox /mg and 0.584, 1.375, 1.200 μmol Trolox /mg, respectively.
Increasing the potency of antihypertensive food-derived peptides is a critical and important step in the development of natural drugs for cardiovascular diseases prevention. We have proposed the egg-white protein precipitate (EWPP) obtained as a byproduct of cystatin and lysozyme isolation as a potential source of ACE-inhibitory peptides derived by pepsin digestion. The results indicated that hydrolysis of EWPP with pepsin produced the ACE inhibitory activity. During 3-h hydrolysis (DH: 38.3%), the IC50 value of EWPP hydrolysate was signifi cantly increased and fi nally reached IC50=643.1 μg/mL. This hydrolysate was further fractionated by RP-HPLC. The peptide fraction exhibiting the highest ACE inhibitory activity was rechromatographed. Three peptide subfractions exhibiting ACE-inhibitory activities of 69.0, 25.0, and 37.6 μg/mL were further characterised. In each of them, mixtures of peptides with different molecular masses were observed.
Lentil meal proteins were treated by chymotrypsin. Hydrolysis was controlled with the pH-stat method. Degree of hydrolysis (DH) was evaluated and after 120 min of the process amounted to 13%. SDS-PAGE and SE-HPLC methods were used to study molecular weight distribution of lentil meal proteins and their chymotryptic hydrolysates of DH 2%, 4%, 8% and 12%. Bands in the range of 21–66 kDa were predominant on the electrophoregram of lentil proteins. Chymotrypsin treatment resulted in releasing the hydrolysis products of both high molecular weight (62,000; 30,500 Da) molecules and small peptides (<6,500 Da). At the first stage of hydrolysis (DH 2.0%) intermediate products are formed, which are then further hydrolysed. Chromatographic separation confirmed the results of SDS-PAGE. Larger polypeptides and unhydrolysed proteins are present in hydrolysate of DH 12% but products of hydrolysis with molecular weight of 0.5–6.5 kDa are predominant. No simple correlation between degree of hydrolysis and intensity of bitterness and astringency sensation was noticed. Bitterness of hydrolysates was not high (2.25-2.35 a.u.).
Starch hydrolysates were prepared by hydrolysis of potato and corn starch mixture with a heat-stable bacterial alpha amylase (Termamyl 120 LS) or with a heat-stable bacterial alpha amylase (Termamyl 120LS) and next with a fungal alpha amylase (Finizym 1600L). Additionally so-called filtration enzyme action was applied (Finizym, Neutrase, Lecitase, SP 348, Gammazym LPL). Introduction of these enzymatic preparations influenced on the increase of filtration rate of hydrolysates and decrease of their viscosity and transmittance value. “Filtration enzyme” did not influence on the carbohydrate composition.
The manuscript presents methodology of obtaining a hydrolysate from ground oat grain under laboratory conditions. The methods applied involved the application of the enzymatic hydrolysis of starch with the use of a thermostable amylolytic preparation Nervanaze T. Parameters of the hydrolysis process were determined by means of acidic inactivation that enables obtaining an oat hydrolysate with a glucose equivalent DE 5.5±0.5 and 4-5% of health-promoting β-glucans applicable mainly as fat replacers.
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