Development of a Scalable Method for the Isolation and Purification of Recombinant Secretory Phospholipase A2 Expressed in Methylotrophic Yeast  Pichia pastoris

S. Yu. Filkin; N. V. Chertova; A. A. Zenin; A. V. Lipkin; E. G. Sadykhov; A. N. Fedorov

doi:10.1134/S0003683819060085

Development of a Scalable Method for the Isolation and Purification of Recombinant Secretory Phospholipase A2 Expressed in Methylotrophic Yeast Pichia pastoris

Authors: Filkin S.Y.¹, Chertova N.V.¹, Zenin A.A.¹, Lipkin A.V.¹, Sadykhov E.G.¹, Fedorov A.N.¹
Affiliations:
1. Bach Institute of Biochemistry, Fundamental Bases of Biotechnology Federal Research Center, Russian Academy of Sciences
Issue: Vol 55, No 6 (2019)
Pages: 670-676
Section: Article
URL: https://journals.rcsi.science/0003-6838/article/view/153058
DOI: https://doi.org/10.1134/S0003683819060085
ID: 153058

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Abstract

An efficient recombinant strain of the methylotrophic yeast Pichia pastoris was obtained; it produces active phospholipase A2 (PLA2) in a high yield. As a result of three stages of purification, a preparation of ~90% purity was obtained. The results of the evaluation of the reproducibility of chromatographic separation of PLA2 give grounds to consider the developed protocol acceptable for scaling; isolated phospholipase A2 can be used for industrial applications.