Characterization of Aspergillus oryzae Aspartyl Aminopeptidase Expressed in Escherichia coli

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概要

• 論文の詳細を見る

• To characterize aspartyl aminopeptidase from Aspergillus oryzae, the recombinant enzyme was expressed in Escherichia coli. The enzyme cleaves N-terminal acidic amino acids. About 30% activity was retained in 20% NaCl. Digestion of defatted soybean by the enzyme resulted in an increase in the glutamic acid content, suggesting that the enzyme is potentially responsible for the release of glutamic acid in soy sauce mash.

• 社団法人 日本農芸化学会の論文
• 2007-10-23

著者

• WATANABE Jun

  Manufacturing Division, Yamasa Corporation

• MOGI Yoshinobu

  Manufacturing Division, Yamasa Corporation

• Akagawa Takumi

  Manufacturing Division Yamasa Shoyu Corporation

• Yamazaki Tatsuo

  Manufacturing Division Yamasa Corporation

• TANAKA Hisaki

  Manufacturing Division, Yamasa Shoyu Corporation

• Tanaka Hisaki

  Manufacturing Division Yamasa Corporation

• Mogi Yoshinobu

  Manufacturing Division Yamasa Corporation

• Watanabe Jun

  Manufacturing Division Yamasa Corporation:department Of Applied Biological Chemistry Faculty Of Agri

関連論文

• Improved Transformation of the Halo-Tolerant Yeast Zygosaccharomyces rouxii by Electroporation
• Improved Transformation of the Halo-Tolerant Yeast Zygosaccharomyces rouxii by Electroporation
• Loss of Aspergillus oryzae amyR function indirectly affects hemicellulolytic and cellulolytic enzyme production(MICROBIAL PHYSIOLOGY AND BIOTECHNOLOGY)
• Characterization of Aspergillus oryzae Aspartyl Aminopeptidase Expressed in Escherichia coli

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