Open Access. Powered by Scholars. Published by Universities.®

Food Science Commons

Open Access. Powered by Scholars. Published by Universities.®

Articles 1 - 3 of 3

Full-Text Articles in Food Science

Measurement Of Proteins In Milk And Dairy Products, Marie K. Walsh May 1988

Measurement Of Proteins In Milk And Dairy Products, Marie K. Walsh

All Graduate Theses and Dissertations, Spring 1920 to Summer 2023

The purpose of this study was to develop a short, easy procedure to measure five major proteins in milk and to detect concentrations of added protein to dairy products. Combinations of casein or whey protein with nonfat-dry milk were made with concentration ratios from 0:10 to 10:0. Similar mixtures of defatted goat milk with defatted cow milk were prepared. Samples were hydrolyzed in 6 N HCl at 145°C for 4 h and analyzed for amino acid composition. Multiple regression equations were derived to estimate the relative content of whey protein or casein added to nonfat-dry milk and goat milk added …


Development Of Microstructure In Raw, Fried, And Fried And Cooked Paneer Made From Buffalo, Cow, And Mixed Milks, Miloslav Kalab, S. K. Gupta, H. K. Desai, G. R. Patil Jan 1988

Development Of Microstructure In Raw, Fried, And Fried And Cooked Paneer Made From Buffalo, Cow, And Mixed Milks, Miloslav Kalab, S. K. Gupta, H. K. Desai, G. R. Patil

Food Structure

Paneer was made from cow, buffalo, and mixed cow and buffalo milk by coagulation with citric acid at pH 5.5. All milk samples were heated to 90°C. Cow milk was coagulated at this temperature but buffalo and mixed milks were cooled to 70°C before coagulation. Differences in the composition and the treatments of the cow and buffalo milks were reflected in the composition and structure of the paneers. Electron microscopy revealed that raw paneer samples had a granular structure consisting of protein particles having a core-and-lining ultrastructure. Deep-frying in vegetable oil at 175'C for 4-5 min led to the compaction …


The Role Of B-Lactoglobulin In The Development Of The Core-And-Lining Structure Of Casein Particles In Acid-Heat-Induced Milk Gels, V. R. Harwalkar, Miloslav Kalab Jan 1988

The Role Of B-Lactoglobulin In The Development Of The Core-And-Lining Structure Of Casein Particles In Acid-Heat-Induced Milk Gels, V. R. Harwalkar, Miloslav Kalab

Food Structure

Acid-heat-induced gels were obtained by coagulating casein micelle dispersions at 90 C using glucono-and-lactone. The casein micelles used were isolated from raw skim milk by centrifugation, washed free of whey proteins and soluble salts, and dispersed in water or a milk dialyzate. The pH values of the gels varied from 4.7 to 6.3. A core-and-lining ultrastructure developed in casein particles coagulated at pH 5.2 to 5.5 from casein micelle dispersions in the milk dialyzate provided that B-lactoglobulin or whey proteins (10 mg/ml) were added to them prior to coagulation. Addition of B-lactoglobulin to aqueous casein micelle dispersions led to the …