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1.
Food Sci Technol Int ; 19(5): 447-60, 2013 Oct.
Article in English | MEDLINE | ID: mdl-23733810

ABSTRACT

Soy protein isolate is typical vegetable protein with health-enhancing activities. Inulin, a prebiotic no digestible carbohydrate, has functional properties. A mashed potato serving of 200 g with added soy protein isolate and/or inulin concentrations of 15-60 g/kg provides from 3 to 12 g of soy protein isolate and/or inulin, respectively. Currently, no information is available about the possible texture-modifying effect of this non-ionizable polar carbohydrate in different soy-based food systems. In this study, the effect of the addition of soy protein isolate and inulin blends at different soy protein isolate: inulin ratios on the degree of inulin polymerization and the rheological and structural properties of fresh mashed and frozen/thawed mashed potatoes were evaluated. The inulin chemical structure remained intact throughout the various treatments, and soy protein isolate did not affect inulin composition being a protein compatible with this fructan. Small-strain rheology showed that both ingredients behaved like soft fillers. In the frozen/thawed mashed potatoes samples, addition of 30 : 30 and 15 : 60 blend ratios significantly increased elasticity (G' value) compared with 0 : 0 control, consequently reducing the freeze/thaw stability conferred by the cryoprotectants. Inulin crystallites caused a significant strengthening effect on soy protein isolate gel. Micrographs revealed that soy protein isolate supports the inulin structure by building up a second fine-stranded network. Thereby, possibility of using soy protein isolate and inulin in combination with mashed potatoes to provide a highly nutritious and healthy product is promising.


Subject(s)
Cooking , Food, Fortified/analysis , Insulin/chemistry , Solanum tuberosum/chemistry , Soybean Proteins/chemistry , Rheology
2.
Electrophoresis ; 16(1): 39-42, 1995 Jan.
Article in English | MEDLINE | ID: mdl-7537659

ABSTRACT

A rapid and sensitive method of detecting pectinesterase activity following electrophoresis or isoelectric focusing in polyacrylamide gels is described. The method uses ruthenium red and requires no addition of substrate when making the gels, thus obviating direct enzyme-substrate contact during electrophoresis. Because of its versatility, the method can be used in a wide variety of applications, such as plant and microbial taxonomy, enzyme purification and characterization, or as an analytical method in fresh and processed plant technology.


Subject(s)
Carboxylic Ester Hydrolases/analysis , Electrophoresis, Polyacrylamide Gel/methods , Isoelectric Focusing/methods , Plant Proteins/analysis , Densitometry , Pectins , Ruthenium Red/chemistry , Sensitivity and Specificity , Staining and Labeling , Substrate Specificity , Time Factors
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