Multimethod training increases portion-size estimation accuracy.
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Biomedical subjects
Publications and source records attributed to A M Tinsley.
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Changes in cooking requirements and chemical composition of whole and dehulled soybeans, stored in 2 different environments [25 degrees C /75% R.H. (Environment 1) and 38 degrees C /90% R.H. (Environment 2)], were studied. Rate of water absorption and solid losses during cooking were higher for the dehulled soybeans at both storage conditions. However, cooking requirements to achieve the same degree of texture in the cotyledons were similar for whole and dehulled seeds. Cooking time increased with prolonged storage; the effect was more noticeable in samples stored under Environment 2. Samples kept for 6 months required almost twice as much cooking than control samples. Dehulled soybeans had a lower fiber content, relatively higher amounts of protein and fat, but similar amino acid compositions than whole soybeans. Cooking caused losses of carbohydrates and ash and, therefore, significantly increased levels of protein and fat reflected by losses of solids during soaking and cooking. Among the amino acids, only cysteine suffered substantial decrease as a result of cooking. Cooking and storage inactivated 99% and from 20-35% of the trypsin inhibitors, respectively; the latter effect was more accentuated in samples stored under Environment 2.
Dehulled entire soybean cotyledons are required for the preparation of many interesting products. Removing hulls had a dramatic effect on the rate of water uptake during soaking. Maximum uptake was reached in only 3 hr compared to the 12 hr needed by whole beans. This saves time and reduces microbial growth during soaking. The amount of water absorbed by beans, with and without hulls, was similar once corrected for solid losses and surface water. Removal of fibrous shells during dehulling increased both the protein and oil contents by 2 %. Dehulled beans steadily lost solids during soaking. Losses were 8.6 % compared to 0.7 % for whole beans when maximum uptakes were first reached. Ways of avoiding or reducing these losses are discussed.
A low-temperature radiofrequency plasma excited in anhydrous ammonia was used to modify polyethylene substrate surfaces for covalent immobilization of proteins. Electron spectroscopy for chemical application (ESCA) was used for surface characterization of polyethylene to a depth scale of 7 nm. The data revealed that surface modification is extensive and occurs in seconds at low discharge power. Primary amino functionalities were detected on the polyethylene surface and the level is dependent on plasma parameters. 125I-labelled antibodies covalently attached to amino groups via glutaraldehyde allowed the conditions for optimum level of primary amine to be established. Both ESCA data and protein loadings are in excellent agreement.