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A computerized imaging system was used for monitoring the emulsion droplet size distribution. The emulsifying properties of β-lactoglobulin preparation were observed to be affected by the environmental factors (protein concentration, pH, ionic strength) that determine the structure of the protein molecule. Generally, the dvs value decreased with an increase in protein concentration and increased with a decrease in pH from 7.0 to 5.0 or an increase in the ionic strength from 20 to 100 mmol/L NaCl. Heterogenicity of emulsion and size of oil droplets in β-lg-stabilised emulsions increased with a pressure increase from 300 to 600 MPa and pressurisation time lengthening from 10 to 30 min at 300 MPa.
The aim of this work was to evaluate in vitro the effect of replacing 0%, 50%, 75% or 100% of cereal-based concentrate in diets based on lucerne hay with feed blocks containing barley grain or 650 g · kg–1 fresh matter of greenhouse waste fruits (tomato, cucumber, or a 1:1 mixture of tomato and cucumber) on ruminal fermentation, methane production, and bacterial and methanogen population sizes. The type of feed-block showed no effect (p ≥ 0.25). The level of concentrate replacement with blocks did, however, affect (p ≤ 0.042) the pH, CH4 concentration, organic matter degradation rate, total gas, CH4 and total VFA production, acetate/propionate and CH4 /total VFAs ratios, and molar proportions of acetate and butyrate, without changing (p ≤ 0.082) methanogen and total bacteria abundance. Increasing levels of concentrate replacement with feed blocks modified ruminal fermentation, dry matter and neutral detergent fibre digestibility, and had an antimethanogenic effect.
The aim of the research was to study the effect of heating (72°C/15 s, 92°C/60 s) water solutions of milk protein concentrate (pH 7.1), obtained by ultrafiltration, on the enzymatic phase during chymosin activity at 32°C at pH 7.1, 6.6 and 6.0. It was found that heating at 72°C limited the number of peptides released at pH 7.1 by 33.3%, and heating at 92°C - by 25.0%. It was affected by differences in the access of the enzyme to glycosylated K-casein. After reducing pH to 6.6, it was observed that heating both at 72°C and 92°C influenced the limitation of the number of released peptides by 13%. The level of the temperature, however, influenced significant differences in RCT which was longer by 17.0% and 34.0% in the substrates heated to 72°C and 92°C. After reducing pH to 6.0, it was found that heating at 72°C and 92°C limited the number of released peptides by 11.2%. However, significant (p=0.05) elongation of RCT (by 8%) was observed only after heating at 92°C.
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