Enhancement of Transglycosylation Activity of Lysozyme by Chemical Modification(Biological Chemistry)

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概要

• 論文の詳細を見る

• An attempt to enhance the transglycosylation activity of lysozyme was made by chemical modification. Computer simulation of the lysozyme-catalyzed reaction indicated that inhibition of the sugar residue binding to the binding subsite A caused a significant increase in transglycosylation activity. Therefore, the binary modification of Asp 101 and Trp 62 in hen egg white lysozyme was made in order to inhibit the sugar residue binding to subsite A. The modified lysozyme, in which the affinity of the sugar residue to subsite A was decreased by about 2kcal/mol of binding free energy change, increased the amounts of transglycosylation products in comparison with the native lysozyme. In particular, the octamer of N-acetylglucosamine was abundantly produced from the initial substrate, pentamer. The modified lysozyme should be useful for synthesis of oligosaccharides with a high degree of polymerization.

• 社団法人日本農芸化学会の論文
• 1989-10-23

著者

• ARAKI Tomohiro

  Department of Bioscience, School of Agriculture, Tokai University

• TORIKATA Takao

  Department of Bioscience, School of Agriculture, Kyushu Tokai University

• Fukamizo T

  新潟大学 農学部応用生物化学科

• Fukui T

  Faculty Of Agriculture Kinki University

• Fukamizo Tamo

  Department Of Advanced Bioscience Kinki University

• Goto Sachio

  Department Of Biophysical Chemistry Faculty Of Agriculture Kinki University

• Goto Sachio

  Department Of Biochemistry Kinki University School Of Medicine

• Araki T

  Department Of Bioscience School Of Agriculture Kyushu Tokai University

• Araki Tomohiro

  Department Of Bioscience School Of Agriculture Kyushu Tokai University

• Araki Tomohiro

  Department Of Biochemistry School Of Agriculture Kyushu Tokai University

• Torikata Takao

  Department Of Biochemistry School Of Agriculture Kyushu Tokai University

• Fukamizo Tamo

  Department Of Advanced Bioscience Faculty Of Agriculture Kinki University

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