Glycation and Phosphorylation of β-Lactoglobulin by Dry-Heating:  Effect on Protein Structure and Some Properties

DOI Web Site PubMed 被引用文献1件
  • Hirofumi Enomoto
    United Chair of Applied Resource Chemistry, Course of Bioresource Science for Processing, United Graduate School of Agricultural Sciences, Kagoshima University, Kagoshima 890-0065, Japan; Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University, Kagoshima 890-0065, Japan; and Food Technology Research Institute, Division of Research and Development, Meiji Dairies Corporation, 540 Naruda, Odawara, Kanagawa 250-0862, Japan
  • Can-Peng Li
    United Chair of Applied Resource Chemistry, Course of Bioresource Science for Processing, United Graduate School of Agricultural Sciences, Kagoshima University, Kagoshima 890-0065, Japan; Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University, Kagoshima 890-0065, Japan; and Food Technology Research Institute, Division of Research and Development, Meiji Dairies Corporation, 540 Naruda, Odawara, Kanagawa 250-0862, Japan
  • Kentaro Morizane
    United Chair of Applied Resource Chemistry, Course of Bioresource Science for Processing, United Graduate School of Agricultural Sciences, Kagoshima University, Kagoshima 890-0065, Japan; Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University, Kagoshima 890-0065, Japan; and Food Technology Research Institute, Division of Research and Development, Meiji Dairies Corporation, 540 Naruda, Odawara, Kanagawa 250-0862, Japan
  • Hisham R. Ibrahim
    United Chair of Applied Resource Chemistry, Course of Bioresource Science for Processing, United Graduate School of Agricultural Sciences, Kagoshima University, Kagoshima 890-0065, Japan; Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University, Kagoshima 890-0065, Japan; and Food Technology Research Institute, Division of Research and Development, Meiji Dairies Corporation, 540 Naruda, Odawara, Kanagawa 250-0862, Japan
  • Yasushi Sugimoto
    United Chair of Applied Resource Chemistry, Course of Bioresource Science for Processing, United Graduate School of Agricultural Sciences, Kagoshima University, Kagoshima 890-0065, Japan; Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University, Kagoshima 890-0065, Japan; and Food Technology Research Institute, Division of Research and Development, Meiji Dairies Corporation, 540 Naruda, Odawara, Kanagawa 250-0862, Japan
  • Shinichi Ohki
    United Chair of Applied Resource Chemistry, Course of Bioresource Science for Processing, United Graduate School of Agricultural Sciences, Kagoshima University, Kagoshima 890-0065, Japan; Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University, Kagoshima 890-0065, Japan; and Food Technology Research Institute, Division of Research and Development, Meiji Dairies Corporation, 540 Naruda, Odawara, Kanagawa 250-0862, Japan
  • Hideo Ohtomo
    United Chair of Applied Resource Chemistry, Course of Bioresource Science for Processing, United Graduate School of Agricultural Sciences, Kagoshima University, Kagoshima 890-0065, Japan; Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University, Kagoshima 890-0065, Japan; and Food Technology Research Institute, Division of Research and Development, Meiji Dairies Corporation, 540 Naruda, Odawara, Kanagawa 250-0862, Japan
  • Takayoshi Aoki
    United Chair of Applied Resource Chemistry, Course of Bioresource Science for Processing, United Graduate School of Agricultural Sciences, Kagoshima University, Kagoshima 890-0065, Japan; Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University, Kagoshima 890-0065, Japan; and Food Technology Research Institute, Division of Research and Development, Meiji Dairies Corporation, 540 Naruda, Odawara, Kanagawa 250-0862, Japan

書誌事項

公開日
2007-02-22
DOI
  • 10.1021/jf062830n
公開者
American Chemical Society (ACS)

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Beta-lactoglobulin (beta-Lg) was glycated with maltopentaose and subsequently phosphorylated by dry-heating in the presence of pyrophosphate to investigate the structural and functional properties of phosphorylated beta-Lg. The circular dichroism spectra showed that the change of the secondary structure in the beta-Lg molecule by glycation and subsequent phosphorylation was small. The differential scanning calorimetry thermograms of beta-Lg showed that the denaturation temperature of the most stable domain was only slightly affected, whereas the retinol-binding activity of beta-Lg was somewhat reduced by glycation and subsequent phosphorylation. These results indicated that the conformational changes of the beta-Lg molecule by glycation and subsequent phosphorylation were mild. The anti-beta-Lg antibody response was somewhat reduced by glycation, but significant changes were not observed by phosphorylation. Although the stability of beta-Lg against heat-induced insolubility was improved by glycation alone, it was further enhanced by phosphorylation. The calcium phosphate solubilizing ability of beta-Lg was enhanced by phosphorylation following glycation.

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