Mechanisms behind protein-protein interactions in a ß-lg-legumin co-precipitate.

Interactions between pea protein and whey protein isolates in co-precipitates and blends consist of a combination of disulphide bonds, hydrophobic and electrostatic interactions. The present study aims to clarify if the two proteins with free thiols, ß-lactoglobulin (ß-lg) and legumin, played a significant role for these interactions. This study used different reagents to modify the conditions of interactions: N-ethylmaleimide (NEM) was used to block reactive thiols, while NaCl and SDS were used to prevent electrostatic or hydrophobic interactions, respectively. The effects of treatments were studied on protein solubility, structure and stability. SDS had no effect, while NEM and NaCl both had great effect, especially in combination. The results showed that interactions of ß-lg and legumin in both co-precipitates and blends are a synergism of electrostatic interactions and disulphide bonds. Thus, ß-lg and legumin are the main proteins responsible for previously observed interactions in protein isolates of whey and pea.

Biodegradation of expanded polystyrene by mealworm larvae under different feeding strategies evaluated by metabolic profiling using GC-TOF-MS.

The present study investigated the biodegradation of polystyrene (PS) plastic by mealworm (Tenebrio molitor) on different diets followed by untargeted screening of larvae gut intestine tissue and frass (manure and feed residuals) to investigate the existence of polymer-generated organic residues. Three different diets, consisting of PS, rolled barley and water were tested. PS degradation rates ranged from 16% to 23% within 15 days, with no statistical differences in survival rates. The larvae fed with ad libitum barley:PS (20:1 w/w) and water had the highest growth rate, while higher PS consumption was observed for barley:PS of 4:1 w/w. A GC-TOF-MS analysis revealed no contaminating substances in the gut intestine tissue, nor styrene or PS oligomers, whilst several bioactive compounds and traces of alkanes, mostly with small carbon chains, were present. Metabolomics analysis on the collected frass, either on the lipophilic (CHCl3) or the polar fraction (MeOH-H2O) was performed. Styrene and PS oligomers (dimers, trimers) were identified, though in a relatively low total amount, up to a total of 346.0 ng/mg 2,4 di-tert butylphenol was identified in both frass and tissue, coming from the PS polymer (Non-intentionally added substances; NIAS). Finally, in the polar fraction of frass, bioactive molecules (fatty acids, amides) were identified, together with several hydrocarbons, mostly with longer carbon chains. The formation of these substances indicated enzymatic and biochemical activity in the larvae-gut intestine. It was shown that degrading and contaminating organic compounds occur at low levels, in both gut intestine and frass, during bio-degradation of PS.

Milking time and risk of over-milking can be decreased with early teat cup removal based on udder quarter milk flow without loss in milk yield.

Increasing the milk flow rate at which milking is terminated can shorten milking time and increase milking efficiency. The effects on milk yield and composition have not been fully investigated when the take-off is set at the udder quarter level and independent of feeding during milking. The objective of this study was to investigate the effect of 3 take-off levels at the udder quarter level (0.06, 0.3, and 0.48 kg/min) applied with or without feeding during milking on milking time, milk yield, the degree of udder emptying, milk composition, and free fatty acids. In this study, 30 cows were allocated into 6 groups, balanced by lactation number, lactation stage, and milk yield, and subjected to a 3 × 2 factorial arrangement of treatments using a Latin square design. Treatments were applied for 1 wk each. This study demonstrated milking time could be reduced by applying up to a take-off level of 0.48 kg/min on udder quarter level without losing milk yield or compromising milk composition or udder health.

Plasmin digestion of photooxidized milk proteins.

Plasmin-mediated hydrolysis of 6 different milk protein preparations [alpha(S)-casein (alpha(S1) + alpha(S2)), beta-casein, kappa-casein, alpha-lactalbumin, beta-lactoglobulin, and lactoferrin] was found to be very dependent on photooxidation of the said proteins. Changes in plasmin proteolysis were investigated in a peptide-mapping study applying liquid chromatography-mass spectrometry. The changes were seen in the formation of peptides formed by plasmin-mediated hydrolysis after photooxidation, which was initiated with the naturally occurring photosensitizer riboflavin in all the milk protein preparations studied. The changes in the plasmin-mediated hydrolysis of photooxidized proteins are discussed in relation to changes introduced in the protein structure upon photooxidation. Plasmin-mediated hydrolysis of alpha(S)-casein, consisting of a mixture of alpha(S1)- and alpha(S2)-casein and a preparation of beta-casein, was most highly affected by photooxidation, which is in agreement with the fact that those 2 proteins have been found to be most labile toward photooxidation. Changes in the formation of potential angiotensin-I-converting enzyme-inhibitory peptides as well as peptides proposed to have antibactericidal activities by plasmin were observed by oxidation of milk proteins before plasmin-mediated hydrolysis.