Proteins for foods, in addition to providing nutrition, should also possess specific functional properties that facilitate processing and serve as the basis of product performance. Functional properties of proteins for foods connote the physicochemical properties which govern the behavior of protein in foods. This general article collates the published information concerning the major functional properties of food proteins, e.g., solubility, binding properties, surfactant properties, viscogenic texturizing characteristics, etc. The effects of extraction and processing on functional properties and possible correlations between structure and function are discussed, in relation to practical performance in food systems. Modification of proteins to improve functional characteristics is briefly mentioned.

Functional properties of proteins in foods: A survey

Nomenclature of the Proteins of Cows’ Milk—Sixth Revision

Summary Flavours can be among the most valuable ingredients in any food formula. Even small amounts of some aroma substance can be expensive, and because they are usually delicate and volatile, preserving them is often a top concern of food manufacturers. Encapsulation describes different processes to cover an active compound with a protective wall material and it can be employed to treat flavours so as to impart some degree of protection against evaporation, reaction, or migration in a food. Encapsulation of flavours has been attempted and commercialized using many different methods such as spray drying, spray chilling or spray cooling, extrusion, freeze drying, coacervation and molecular inclusion. The choice of appropriate microencapsulation technique depends upon the end use of the product and the processing conditions involved in the manufacturing product. This overview describes each method cited above in terms of the basic chemical and/or physical principles involved and covers mechanisms of flavour release from food matrices.

Flavour encapsulation and controlled release - a review.

Microencapsulation involves the incorporation of food ingredients, enzymes, cells, or other materials in small capsules. Microcapsules offer food processors a means with which to protect sensitive food components, ensure against nutritional loss, utilize otherwise sensitive ingredients, incorporate unusual or time-release mechanisms into the formulation, mask or preserve flavors and aromas, and transform liquids into easily handled solid ingredients. Various techniques are employed to form microcapsules, including spray drying, spray chilling or spray cooling, extrusion coating, fluidized-bed coating, liposome entrapment, coacervation, inclusion complexation, centrifugal extrusion, and rotational suspension separation. Recent developments in each of these techniques are discussed in this review. Controlled release of food ingredients at the right place and the right time is a key functionality that can be provided by microencapsulation. A timely and targeted release improves the effectiveness of ...

Recent Developments in Microencapsulation of Food Ingredients

Nitrate in serum and urine was assayed by a modification of the cadmium-reduction method; the nitrite produced was determined by diazotization of sulfanilamide and coupling to naphthylethylene diamine. After samples were deproteinized with Somogyi reagent, the nitrate was reduced by Cu-coated Cd in glycine buffer at pH 9.7 (2.5 to 3 g of Cd granules for a 4-mL reaction mixture). The reduction followed pseudo-first-order reaction kinetics, a convenient time interval for assay being 75 to 90 min. Maximum reduction (85%) occurred at about 2 h. Detection limits in urine or serum were 2 to 250 mumol/L. This method does not require the reaction to go to completion, does not require expensive reagents or equipment, and can assay several samples simultaneously. Repeated assays of two serum pools gave CVs of 9.0% and 4.7% for nitrate concentrations of 31.4 and 80.2 mumol/L, respectively (n = 20 each). The mean concentration of nitrate was 1704.0 +/- 1294 (SD) mumol/L (n = 21) in untimed normal urine, 81.8 +/- 50.1 mumol/L in serum of 38 renal dialysis patients, and 51.2 +/- 26.4 mumol/L in serum of 38 controls.

S.T. Coulter

Papers

A Modified Peroxide Test for Detection of Lipid Oxidation in Dairy Products

Role of Sulfhydryl Groups in the Interaction of κ-Casein and β-Lactoglobulin1

The effect of the various steps in the manufacture on the extent of serum protein denaturation in nonfat dry milk solids.

Flavor Retention During Drying

Four Factor Response Surface Experimental Design for Evaluating the Role of Processing Variables Upon Protein Denaturation in Heated Whey Systems