Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Masahiko Samoto"'
Publikováno v:
Food Chemistry Advances, Vol 1, Iss , Pp 100115- (2022)
Two existing approaches facilitate the understanding of the role of soy protein in maintaining soybean product quality: the first involves the separation of the major protein fractions from the soybean seeds via various techniques, whereas the second
Externí odkaz:
https://doaj.org/article/dd493e76247d49c39e7fbc7a8e327c67
Autor:
Jiraporn Sirison, Toya Ishii, Kentaro Matsumiya, Yuki Higashino, Yuko Nambu, Masahiko Samoto, Masahiro Sugiyama, Yasuki Matsumura
Publikováno v:
Food Hydrocolloids. 141:108745
Autor:
Yuko Nambu, Masanobu Yanagisawa, Kentaro Matsumiya, Toya Ishii, Yasuki Matsumura, Masahiko Samoto
Publikováno v:
Food Structure. 12:64-72
Soybean oil bodies are natural and environment-friendly emulsifying agents from plant resources required as a substitute for emulsifiers such as low-molecular-weight one and animal proteins. The aim of this study was to reveal the interfacial propert
Autor:
Jiraporn Sirison, Toya Ishii, Mitsutaka Kohno, Kentaro Matsumiya, Yasuki Matsumura, Masahiko Samoto
Publikováno v:
Food Hydrocolloids. 112:106345
Soy lipophilic protein (LP) is considered to form a major fraction of soy protein isolate, in addition to β-conglycinin (7 S) and glycinin (11 S). LP consists of phospholipid-protein complex and phospholipid-free protein molecules. Surface and foami
Autor:
Hiroshi Hidaka, Jiraporn Sirison, Mitsutaka Kouno, Yasuki Matsumura, Masahiko Samoto, Kentaro Matsumiya
Publikováno v:
Bioscience, biotechnology, and biochemistry. 81(4)
Solubility of soy lipophilic proteins (LP) was studied as compared with that of other soy protein fractions. LP, β-conglycinin, glycinin, and soy protein isolate (N-SPI) were prepared under the condition to avoid heat denaturation. Solubility of LP
Autor:
Koji Takahashi, Masahiko Samoto, Yukio Kawamura, Hideaki Tsuji, Tadashi Ogawa, Miki Hiemori, Kohsei Tabuchi, Yoichi Fukuda
Publikováno v:
Bioscience, biotechnology, and biochemistry. 61(12)
A wild-type soybean contains three major allergenic proteins, Gly m Bd 30K, the α-subunit of conglycinin, and Gly m Bd 28K. A genetically mutated soybean (Tohoku 124), which was originally developed as a cultivar lacking the α- and α'-subunits of
Publikováno v:
Bioscience, biotechnology, and biochemistry. 62(5)
The precipitate formed by ultracentrifuging a defatted soybean extract at 200,000×g for 50 min at pH 7.5 was composed of particles of 100-200 nm in diameter and enriched with 34-kDa, 24-kDa and 18-kDa proteins. An SDS-PAGE analysis showed these prot
Autor:
Rie Ito, Yukihiro Nakabou, Masahiko Samoto, Mitsutaka Kohno, Takashi Koikeda, Motohiko Hirotsuka, Motohiro Maebuchi
Publikováno v:
Food Science and Technology Research. 13:45-53
In this study, we compared the intestinal absorption from different sources with the same amino acid composition (protein, peptide, and amino acid mixture) by measuring changes in serum concentrations of various amino acids. Peptides used in this stu
Publikováno v:
Journal of Nutritional Science and Vitaminology. 46:271-279
About 15 soybean proteins were shown to be recognized by sera of soybean-sensitive patients with atopic dermatitis. Three of them were identified as major allergens and designated as Gly m Bd 60K, Gly m Bd 30K, and Gly m Bd 28K, respectively. Gly m B
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 60:1006-1010
When defatted soy milk was ultracentrifuged, 34kDa allergenic soyabean protein Gly m Bd 30 K was more abundant in the precipitate than in the supernatant by an SDS-PAGE analysis. The addition of more than 10 mM of 2-mercaptoethanol (2-ME) to the soy