![Sample our Food Science & Technology journals, sign in here to start your access, latest two full volumes FREE to you for 14 days]({"type":"image" , "src" : "/sda/5936/TOC-Subject-Sample-2021-Food-Science-Technology.jpg"})
Abstract
Beer proteins of molecular weight 10,000–50,000 were separated from a closely associated surface-active fraction by chromatography on Duolite A392. The fraction that was not retained showed no surface activity. The retained fraction demonstrated surface activity and contained nitrogen and carbohydrate but did not exhibit characteristic properties of proteins when analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis or isoelectric focusing. The fluorescent and ultraviolet-visible spectra of this fraction were similar to the spectroscopic properties of melanoidins and nonenzymatically glycosylated proteins.