1,5-Anhydro-D-fructose, a New Material for Modification of Amino Groups as Demonstrated Using Amino Acid and Proteins.
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- Yoshinaga Kazuhiro
- The United Graduate School of Agricultural Sciences, Kagoshima University
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- Fujisue Mami
- Nihondenpun Kogyo Co.
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- Abe Jun-ichi
- Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University
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- Takeda Yasuhito
- Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University
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- Hizukuri Susumu
- Faculty of Home Economics, Kobe Women's University
Bibliographic Information
- Other Title
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- 新しいアミノ基の修飾剤,1,5-アンヒドロ-D-フルクトースによるアミノ酸と蛋白質の修飾
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Abstract
1, 5-Anhydro-D-fructose (1, 5-anhydro-D-arabino-hexo-2-close, 1, 5-AF) reacted well with the amino group and seemed to be useful as a reagent for modification of the amino compounds. The rate of browning of 1, 5-AF by reaction with glycine was higher than those of glucose and xylose at 50°C and pH 7.5. Forty-five percent of the amino group of glycine was modified by the incubation of a lyophilized mixture of 1, 5-AF and glycine at 30°C for 48 h, whereas the degree of modification by glucose was less than 5%. This modification was applied to lysozyme. A mass spectrum indicated that the sugar moiety was incorporated into the lysozyme. The optimum pH values of the modified and unmodified lysozyme on glycolchitin were pH 4.5 and 5.0, respectively. On the other hand, the optimum pH of the modified enzyme on freeze-dried cells of Micrococcus lysodeikticus shifted from pH 7.8 to 6.0. Wheat proteins, gliadin and glutenin, were also modified. The modified gliadin had higher emulsification ability and solubility than the unmodified ones.
Journal
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- Journal of Applied Glycoscience
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Journal of Applied Glycoscience 49 (2), 129-135, 2002
The Japanese Society of Applied Glycoscience
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Details 詳細情報について
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- CRID
- 1390282681270239232
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- NII Article ID
- 10008253529
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- NII Book ID
- AN10453916
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- ISSN
- 13403494
- 18807291
- 13447882
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- NDL BIB ID
- 6142360
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- Text Lang
- en
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- Data Source
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- JaLC
- IRDB
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed