• Korean Journal of Food Science and Technology
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• v.22 no.7
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• pp.805-811
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• 1990

Hydrolysis of soybean proteins was carried out by immobilized trypsin and/or alpha-chymotrypsin. The partially hydrolyzed products of soybean proteins were evaluated for their molecular weights and molecular charges by using Ferguson's plot. The ratio of average molecular weights to average molecular charges($\bar{M}/log\;\bar{Y}_o$) of modified soybean proteins could be used to predict functional properties such as solubility, water holding capacity, oil holding capacity, and emulsifying ability. The low ratio of modified soybean proteins indicated high solubility. while the high ratio showed high water holding capacity. The appropriate ranges of the ratios were necessary for maximun oil holding capacity and emulsifying ability.

• Parasites, Hosts and Diseases
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• v.29 no.2
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• pp.113-120
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• 1991

When the component proteins in crude saline extract of 13-week old adult Paragonimus westermani were observed by non-denaturing discontinuous-polyacrylamide gel electrophoresis (Disc-PAGE), 8 distinct bands were clearly recognized. Molecular weight (MW) of each band protein, numbered in sequence from cathodal side which appeared in 10% separating gel, was measured first by Ferguson plot utilizing different gel concentrations from 10% to 4.5%. MW of band 1 Protein (known as egg Protein) was 440 kDa. And MW of other band Proteins were: 386 kDa in band 2, 17.4 kDa in band 3, 17kDa in band 4, 14.3 kDa in band 5, 46 kDa in band 6, 38 kDa in band 7 and 23 kDa in band 8. When the proteins in the crude extract were separated into fractions by molecular sieve chromatography through 1.6 (Φ)×70cm sired Sephacryl 5-300 Superane column and revisualized by Disc-PAGE in 8% gel, the sequence of fluted proteins was band 1, band 2, band 6, band 7 and bands 3,4,5 and 8. This elusion profile confirmed MW of each band protein in the crude extract as measured by Ferguson plot.