Forty-one volatile components were identified from an extract of carambolas by using a capillary gas chromatograph-mass spectrometer combination. The most prominent aroma was grape-like, and methyl anthranilate was the most abundant component. The strong fruity aroma of the extract is probably due to the major esters and ketones in the extract. Carambolas are consumed mostly as fresh fruit and have recently progressed from a dooryard ornamental to small commercial plantings of one or two selected cultivars (Brooks, 1983). The unique star-shaped fruit vary in color from white to dark yellow. The yellow varieties have more commercial appeal because the deeper yellow color is more attractive to the consumer. The white varieties have been reported to be sweeter than the yellow varieties (Harler, 1983). Wagner et al. (1975) reported ascorbic and oxalic acid content, acidity, Brix, and taste panel evaluation for carambolas that were mostly of the yellow varieties. Flavor attributes ascribed to some of these were sweet, good, and apple-like, sour, tart, and apple-like, and sweet, good, and mild. Others have suggested carambolas have an apricot-like flavor (Harler, 1983). Little information on the chemical composition of carambolas is available, and to date, no reports on volatile flavor components of carambolas have been published. Information on chemical composition will be useful to plant breeders and horticulturists for plant breeding studies and to food processors and fresh product suppliers in selecting varieties for marketing and processing. The current study reports volatile components of carambola and discusses the importance of individual components as contributors to its flavor. An immobilized enzyme reactor system consisting of D-amino acid oxidase and catalase coimmobilized on porous succinamidopropyl-glass beads was examined with regard to its function in a method for determination of amino acid racemization in proteins. The extent of racemization was measured from the reduction in the amount of an amino acid, as determined by chromatographic analyses, following treatment of an acid hydrolysate with the immobilized enzyme reactor. Racemization rates resulting from alkaline heat treatments (0.2 N NaOH, 40 °C) of five proteins (soy isolate, wheat isolate, α-lactalbumin, bovine serum albumin, and β-lactoglobulin) indicated that, although the rates varied between proteins, the relative rate of phenylalanine racemization was constant and roughly double that for alanine. Racemization of tyrosine occurred at a rate similar to that of alanine; however, that for isoleucine, leucine, and valine was barely detectable following a 20-h incubation.