ABSTRACTA Maillard complex of bovine serum albumin and D‐glucose was prepared by equilibrating a freeze‐dried mixture of the protein and sugar at 52 relative humidity followed by heating at 55°C for 18 hr. No visible brown pigmentation was observed in the resulting powder. An 80 reduction in free amino groups was measured during the heating period. Solutions of the protein and the protein‐sugar complex were heated for 30 min at temperatures ranging from 60–100°C. The heated albumin was insoluble at the isoelectric pH while the albumin‐glucose complex maintained solubility over a pH range of l‐7. Increases in levorotation due to heat treatment were similar for the protein and the protein‐sugar complex. These results indicate that the complexing of bovine serum albumin with D‐glucose increases the stability of the protein by protection against precipitation of the denatured molecules rather than protection against changes in inter
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