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Literature summary for 1.4.3.3 extracted from

  • Zheng, H.; Wang, X.; Chen, J.; Zhu, K.; Zhao, Y.; Yang, Y.; Yang, S.; Jiang, W.
    Expression, purification, and immobilization of His-tagged D-amino acid oxidase of Trigonopsis variabilis in Pichia pastoris (2006), Appl. Microbiol. Biotechnol., 70, 683-689.
    View publication on PubMed
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Application

Application Comment Organism
synthesis intracellular production of HDAO under P(GAP), followed by affinity purification and immobilization on oxirane resin, may serve as an effective process for the manufacture of immobilized DAO for industrial application Trigonopsis variabilis

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged DAO (HDAO) in Pichia pastoris using the glyceraldehydes-3-phosphate dehydrogenase promoter. The maximal level of HDAO expression using the P(GAP) integrant is attained in 13 h and is equal to that obtained using the P(AOX1) integrant in 43 h.In-frame fusion of Saccharomyces cerevisiae alpha-factor secretion signal under a P(GAP) or P(AOX1) results in low-level secretion of active HDAO, which is not of practical use Trigonopsis variabilis

General Stability

General Stability Organism
enzyme immobilized on Amberzyme oxirane resin can be recycled more than 14 times without significant loss of activity Trigonopsis variabilis

Organism

Organism UniProt Comment Textmining
Trigonopsis variabilis
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Purification (Commentary)

Purification (Comment) Organism
enzyme intracellularly expressed under P(GAP) integrant in Pichia pastoris Trigonopsis variabilis