High-level secretory production of phospholipase A1 by Saccharomyces cerevisiae and Aspergillus oryzae

Yoichiro Shiba, Chiho Ono, Fumio Fukui, Ichiro Watanabe, Nobufusa Serizawa, Katsuya Gomi, Hiroji Yoshikawa

Research output: Contribution to journalArticlepeer-review

25 Citations (Scopus)


Phospholipase A1 (PLA1) is a hydrolytic enzyme that catalyzes the removal of the acyl group from position 1 of lecithin to form lysolecithin. The PLA1 gene, which had been cloned from Aspergillus oryzae, was expressed in Saccharomyces cerevisiae and A. oryzae. Through the modification of the medium composition and the feeding conditions of substrate, the production level of PLA1 by S. cerevisiae was increased to a level fivefold higher than that indicated in a previous report. In the case of A. oryzae, introduction of multicopies of PLA1 expression units, and the morphological change from the pellet form to the filamentous form were effective for the enhancement of PLA1 production. We succeeded in producing 3,500 U/ml of PLA1 using an industrial-scale fermentor.

Original languageEnglish
Pages (from-to)94-101
Number of pages8
JournalBioscience, Biotechnology and Biochemistry
Issue number1
Publication statusPublished - 2001 Jan


  • Aspergillus oryzae
  • CPY
  • Mycelial morphology
  • Phospholipase A
  • Saccharomyces cerevisiae

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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