Biomedical subjects

Marcela Alexander

Publications and source records attributed to Marcela Alexander.

4 recordsLinked to original sources

PubMed2005

Interactions between denatured milk serum proteins and casein micelles studied by diffusing wave spectroscopy.

The acid-induced aggregation of casein micelles from milk, in the presence of different whey protein preparations from heated and unheated milk, has been studied using diffusing wave spectroscopy (DWS). In particular, the study focused on the turbidity (or l*) parameter obtainable from DWS, which can give information on the interactions between particles in aggregating systems. The experiments provided evidence that the presence of small, soluble, whey protein/kappa-casein aggregates derived from heated milk gave rise to interactions with both heated and unheated casein micelles over a pH range of 5.6 down to 5.2. Comparison of heated and unheated milks, together with milks whose sera had been exchanged, showed that direct interactions were indeed occurring, even between untreated casein micelles and soluble whey protein complexes. Comparison of the behavior of the whey protein aggregates in emulsion preparations where they could not interact with the large particles confirmed that the effect was specific to the presence of casein micelles and could not arise simply from the aggregation of the whey proteins themselves.

Caseins↗

PubMed2005

Stabilization of caseinate-covered oil droplets during acidification with high methoxyl pectin.

Polysaccharides are widely used in the food industry to modify the stability of protein-based drinks. However, an in depth knowledge of the interactions occurring in the system is still lacking. In this study, the interactions between sodium caseinate and high methoxyl pectin under acidification conditions were studied nondestructively and without dilution using transmission diffusing wave spectroscopy. Oil-in-water emulsions were prepared with 10% soybean oil and 0.5% sodium caseinate. Various concentrations of pectin (ranging from 0 to 0.2%) were added, and the emulsions were acidified with glucono-delta-lactone. With acidification, a "sol-gel" transition occurred and emulsions containing pectin were more stable at lower pH than those without pectin. Furthermore, the sol-gel transition of the mixtures was more sudden for control emulsions without pectin. While in control samples the final solidlike emulsion after gelation tended to be more inhomogeneous and more dissimilar to the starting emulsion, emulsions with pectin in solution gelled later under acidification. With a sufficient amount of pectin, the emulsions showed no aggregation and the destabilization pH varied depending on the amount of pectin present in the emulsions. At intermediate pH values (pH > 5.5), the emulsions displayed a decrease in particle size, more pronounced in samples containing pectin. The results collected using light scattering in concentrated systems, 10% (v/v) in our case, suggested that pectin stabilizes the emulsion oil droplets forming a network of oil droplets loosely connected by strands of pectin.

Caseins↗

PubMed2005

Interactions of high methoxyl pectin with whey proteins at oil/water interfaces at acid pH.

The interactions between whey protein isolate (WPI) and high methoxyl pectin (HMP) at pH 3.5 were investigated in situ using ultrasound (US) and diffusing wave spectroscopy (DWS). HMP was added to 10% oil-in-water emulsions containing 1% WPI. At neutral pH, no protein-pectin interactions were observed as both molecules are negatively charged, while at pH 3.5 bridging flocculation occurred via electrostatic interactions. Four different stages were distinguished during the addition of HMP in WPI-stabilized emulsions at pH 3.5. At a concentration below a critical value, no interactions were observed. At concentrations >0.02% HMP, a change in the l factor indicated a change in the ordering of the emulsion droplets, influenced by long-range interactions. At higher concentrations (in the range between 0.04 and 0.06% HMP), attenuation showed significant changes in the surface of the oil droplets, changes which affected the droplet-droplet interactions. At pectin concentrations >0.05%, attenuation of sound and 1/l* decreased, while velocity of sound and particle size increased, as a result of bridging flocculation. These results demonstrated for the first time that methods such as US and DWS combined permit the observation of the early stages of the interactions between two biopolymers at the interface. This is significant in light of increasing efforts in engineering complex interfacial layers.

Chemical Phenomena↗

PubMed2004

Application of transmission diffusing wave spectroscopy to the study of gelation of milk by acidification and rennet.

Transmission diffusing wave spectroscopy has been used to study and compare three milk gelling systems (acid gelation of heated and unheated milks and rennet coagulation of unheated milk). In all cases, DWS was able to demonstrate the point of gelation as indicated by a rapid increase in particle size, as well as the small decreases in casein micelle radius attributed to the collapse or removal of the hairy kappa-casein layer. More importantly, the photon transport mean free path (l(*)) was measured. This parameter is unique to transmission DWS and can potentially give information about developing microstructures and the mechanical properties between different types of gels. The values of l(*) changed during the gelation processes, and these changes were manifested earlier than any change in particle aggregation or rheology of the systems. All three different gelling systems showed different changes in l(*) with time, showing the development of different interactions as the acidification or renneting reactions proceeded. Although a full analysis of the l(*) parameter and its changes cannot be made, it is concluded that they can provide important information on the pre-gelation states of aggregating systems.

Animals↗