Enzymatic Modification of Protein Functionality: Implantation of Potent Amphiphilicity to Succinylated Proteins by Covalent Attachment of Leucine Alkyl Esters
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概要
- 論文の詳細を見る
This work is a new attempt to modify the functionality of food proteins by the use of a potential activity of papain. Fish protein concentrate, soy protein isolate, casein, ovalbumin and gelatin were succinylated prior to using them as substrates. Each of the L-leucine n-alkyl esters with different alkyl-chain lengths was covalently incorporated into each substrate by applying the unusual papain-catalyzed reaction [Agric. Biol. Chem., 43, 1065 (1979)]. The resulting products posessed high whippability and/or emulsifying activity. The highest whippability was observed when leucine butyl ester or hexyl ester was incorporated, while the incorporation of higher alkyl esters generally caused an increase in emulsifying activity.
- 社団法人 日本農芸化学会の論文
著者
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Shimada Atsuko
Department Of Biological Science Graduate School Of Science University Of Tokyo
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Arai Soichi
Department Of Agricultural Chemistry Faculty Of Agriculture The University Of Tokyo
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Watanabe Michiko
Department Of Agricultural Chemistry The University Of Tokyo
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ARAI Soichi
Department of Agricultural Chemicatry, The University of Tokyo
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