Biotechnology Letters

, Volume 25, Issue 10, pp 827–831

Comparison of extracellular Escherichia coli AppA phytases expressed in Streptomyces lividans and Pichia pastoris

Article

DOI: 10.1023/A:1023568826461

Cite this article as:
Stahl, C.H., Wilson, D.B. & Lei, X.G. Biotechnology Letters (2003) 25: 827. doi:10.1023/A:1023568826461

Abstract

A phytase gene (appA) from Escherichia coli was cloned into Streptomyces lividans and expressed as an extracellular protein which was then compared with the same enzyme expressed in Pichia pastoris. The phytase expressed in S. lividans was not glycosylated and had a molecular mass of 45 kDa. Compared with the glycosylated phytase expressed in P. pastoris, this non-glycosylated phytase was 25–50% less active (p<0.05) at pH 2 to 3.5 or at 45 and 55 °C, but 50% more active (p<0.05) at 75 °C. The thermo-tolerance of the non-glycosylated phytase was 26 and 48% higher (p<0.05) than that of the glycosylated phytase at 45 and 55 °C, but was 80 and 94% lower (p<0.05) at 65 ° and 75 °C, respectively.

enzyme expressionEscherichia coliphytasePichia pastorisStreptomyces lividans

Copyright information

© Kluwer Academic Publishers 2003

Authors and Affiliations

  • Chad H. Stahl
    • 1
    • 2
  • David B. Wilson
    • 2
  • Xin Gen Lei
    • 4
  1. 1.Department of Animal ScienceUSA
  2. 2.Department of Molecular Biology and GeneticsCornell UniversityIthacaUSA
  3. 3.Department of Animal ScienceIowa State UniversityAmesUSA
  4. 4.Department of Animal ScienceCornell UniversityIthacaUSA