MISC

2020年4月3日

Novel activity of Streptomyces aminopeptidase P

Bioresources and Bioprocessing
  • Wan Kun
  • ,
  • Uraji Misugi
  • ,
  • Yang Lingli
  • ,
  • Nakahigashi Ryota
  • ,
  • Hatanaka Tadashi

7
1
開始ページ
20
終了ページ
20
記述言語
英語
掲載種別
出版者・発行元
SpringerOpen

Streptomyces aminopeptidase P enzymes are proline-specific peptidases that belong to the peptidase M24 family. To evaluate the activity of a commercial Streptomyces aminopeptidase P, named 'XPO DUET', we performed three experiments involving degradation of tryptic casein, production of free amino acids from casein hydrolysate, and hydrolysis of synthetic peptides. Using an ion-trap liquid chromatography-mass spectrometry (LC-MS) apparatus, we demonstrate that XPO DUET could degrade FFVAPFPEVFGK, an allergic and bitter peptide, VAPFPEVFGK, and PEVFGK from tryptic casein. All amino acids, except Ala, Asp, Glu, and Tyr, were released in an XPO DUET activity-dependent manner during the hydrolysis of casein hydrolysate. LC-MS analysis also revealed the ability of XPO DUET to completely hydrolyze Phe-Phe-Phe into free Phe. Thus, we confirm that XPO DUET possesses broader specificity than its known activity toward Xaa-Pro peptides. Because XPO DUET is a food-grade peptidase, it is useful in the bioprocessing of protein hydrolysates through its combination with other food-grade peptidases.

リンク情報
CiNii Articles
http://ci.nii.ac.jp/naid/120006840181
URL
http://www.lib.kobe-u.ac.jp/handle_kernel/90007037
ID情報
  • ISSN : 2197-4365
  • CiNii Articles ID : 120006840181

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