Plant-based beverages (PBB) are often marketed and used by consumers as alternatives to ruminant milks, particularly bovine milk (hereafter referred to as milk). However, much research has established that there is variation in nutritional composition among these products, as well as demonstrating that they are largely not nutritional replacements for milk. A survey of the prices and nutrition labels of PBB available in New Zealand supermarkets was undertaken.
View Article and Find Full Text PDFThis study investigated the structural and physicochemical changes that occur in milk, a naturally designed complex structured emulsion, during gastric digestion using the bottle-fed piglet as an animal model. The gastric digestions of cow, goat, and sheep milk were compared in male piglets euthanized at different postfeeding times to collect the stomach chyme. The cow and noncow milks separated into curd (aggregated caseins) and liquid (mostly soluble whey) phases in the piglet's stomach.
View Article and Find Full Text PDFThis study investigated the structural characteristics of oil bodies from mature coconut (Cocos nucifera L.) fruit. The ultrastructure and the distribution of oil bodies in coconut endosperm were investigated using cryo-scanning electron microscopy.
View Article and Find Full Text PDFIn this study we investigated the effects of different levels of glucosylation and lactosylation on β-Lg self-assembly into nanofibrils at 80 °C and pH 2. Fibrils in heated samples were detected with the thioflavin T assay and transmission electron microscopy, while SDS-PAGE was used to investigate the composition of the heated solutions and fibrils. Glycation had different effects in the nucleation and growth phases.
View Article and Find Full Text PDFβ-Lactoglobulin (β-lg) forms fibrils when heated at 80 °C, pH 2, and low ionic strength (<0.015 mM). When formed at protein concentrations <3%, these fibrils are made up of peptides produced from the acid hydrolysis of the β-lg monomer.
View Article and Find Full Text PDFBovine β-lactoglobulin (β-Lg) self-assembles into long amyloid-like fibrils when heated at 80 °C, pH 2, and low ionic strength (<0.015 mM). Heating β-Lg under fibril-forming conditions shows a lag phase before fibrils start forming.
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