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Precursors to Nitrosopyrrolidine and Nitrosopiperidine in Black Pepper Treated with Nitrous Acid
Authors:Masamichi Nakamura  Kuni Katoh  Toshiharu Kawabata
Institution:1. Department of Food and Drug Science, Kanagawa Prefectural Public Health Laboratory, 52–2 Nakao-cho, Asahi-ku, Yokohama, 241, Japan;2. Department of Biomedical Research on Food, National Institute of Health of Japan, 2–10–35 Kamiosaki, Shinagawa-ku, Tokyo 141, Japan
Abstract:The following properties of food proteins polymerized by guinea pig liver transglutaminase were investigated: (1) solubility, (2) emulsifying activity and emulsion stability, and (3) unfrozen water content by pulsed NMR. Several food proteins (αsl- and k-caseins, and soybean 7S and 11S globulins) were polymerized by this enzyme. Solubility and emulsifying activity of polymerized αsl-casein were higher than those of the native protein in the range of pH 4~6. Unfrozen water contents of polymerized soybean globulins were much higher than those of the native proteins. These results suggest that transglutaminase treatment may be used for the production of new food protein material with higher hydration ability.
Keywords:surface layer  Bacillus sphaericus  pathogenic  crystal lattice  toxicity
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