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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.).
The aim of the study was to recognize the polymorphism in the calpastatine genes (CAST/Hindi and CAST/Hpy188I) and in the ryanodine receptor gene (RYR1) as well as to establish a possibile linkage between the genes variants and carcass and pork quality traits in crossbreds of German Landrace × German Large White or Leicoma × German Large White sows with Pietrain boars. In terms of carcass and pork quality, no significant differences were found between the genotypes CT and CC at the locus RYR1, as well as between AA and AB genotypes at the locus CAST/Hpy188I. On the other hand, a significant effect was identified of the CAST/HinfI polymorphism on pork quality traits. The meat of AB pigs showed a significantly higher pH, lower drip loss and thermal drip,lower WHC, and lower redness and yellowness of colour as compared to BB animals. Furthermore,a significant effect of interaction CAST/HinfI × RYR1 was found in relation to WHC of meat. The results presented indicate that the CAST gene polymorphism identified by HinfI enzyme may be considered important in terms of meat quality traits of the analysed crossbreds. A follow-up study is necessary, however, involving a larger population that would represent all possible genetic variants of the CAST.
Cruciferin was separated from the rapeseed crude proteins using salting out with ammonium sulphate and Sephadex G-200 gel filtration. Then, so obtained protein fraction was separated using a micellar electrokinetic chromatography (MEKC) with SDS as a the surfactant. Nine peaks with migration times between 14.33 and 20.48 min were recorded on the chromatogram. The main cruciferin subfractions were characterised with molecular mass of 22 000 and 33 000 determined using MEKC technique. UV spectra showed that cruciferin protein appears as a complex with phenolic acids.
The aim of this study was to determine the effect of the calpastatin (CAST) and ryanodine receptor (RYR1) genes polymorphism on carcass and meat quality traits in Pietrain crossbred pigs. No significant differences in the traits examined were identified between pigs with the genotypes CT and CC at the locus RYR1. A significant association occurred between the polymorphisms CAST/PvuII and CAST/RsaI, and the traits characterizing the quality of carcass and composition of meat. Meat from pigs with the genotype AB CAST/PvuII had a significantly higher pH determined 24 and 48 h post mortem, lower drip loss, lower yellowness (b*) and a lower protein content compared to meat from pigs with the genotype AA. In addition, the meat from pigs with the genotype EF CAST/RsaI had a significantly higher pH 48 h post mortem, lower drip loss and lower yellowness (b*) than that of pigs with the genotype EE. The results indicate that several quality and composition traits of fresk meat from the offspring by Pietrain boars are significantly related to the CAST genotype.
The aim of this study was to determine the association between polymorphism located in exon 8 of PPARGC1A gene (Cys430Ser) and carcass quality in pigs. Experiment was carried out on 350 PIC hybrid fatteners. Polymorphism was analyzed using PCR-RFLP method. The frequency of genotypes was as follows: AA – 0.33, AT – 0.57, TT – 0.1, however alleles: A – 0.62, T – 0.38. In the analyzed population loss of Hardy-Weinberg equilibrium was observed (P ≤ 0.01). Statistical analysis showed that only one of the evaluated traits was associated with individual PPARGC1A genotypes. Cooling loss value for pig carcasses with TT genotype was statistically significant (P ≤ 0.05) higher than observed in those with AA and AT genotypes.
Reversed-phase HPLC of liberated hippuric acid (HA) from an ACE assay in the presence of ACE inhibitory peptides derived from a crackling hydrolysate was conducted. The efficacies of two different analytical HPLC columns using identical mobile phases with an isocratic system were tested. Chromatograms revealed that the shorter C8 column (4.6 × 150 mm, 5 μm) was just as efficient as the longer C18 column (4.6 × 250 mm, 5 μm) in resolving liberated HA, but achieved this in a much shorter time (i.e., 3.67 cf 12.52 min). The presence of the crackling hydrolysate exhibited ACE-inhibiting activity by retarding the liberation of HA from the substrate hippuryl-L-histydyl-L-leucine (HHL) in a dose-dependent manner, and did not interfere with the chromatography. Hence, a quick reliable analytical methodology is at hand for the in vitro examination of various “bioactive peptide concoctions” for possible use in the development of functional foods.
Phenolic compounds from the leaves of the bearberry plant (Arctostaphylos uva-ursi L. Sprengel) were extracted into 95% (v/v) ethanol. Tannin fractions were obtained by Sephadex LH-20 column chromatography using 50% (v/v) acetone as the mobile phase. The tannin fraction was then further characterised by size exclusion high-performance liquid chromatography (SE-HPLC) on a TSK G2000SWXL column with a mobile phase comprising 45% acetonitrile and 0.1% (v/v) TFA. The chromatography revealed the presence of additional phenolic compounds in the tannin fractions which are not proanthocyanidins (i.e. condensed tannins).
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