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Purification and Characterization of Recombinant Streptomyces Griseus Aminopeptidase

Purification and Characterization of Recombinant Streptomyces Griseus Aminopeptidase

Sally Xueying Ni, Douglas Cossar, Adrian Man, Karen Norek, David Miller, Craig Kearse, Vadim Tsvetnitsky

Protein Expr Purif. 2003 Jul;30(1):62-8.

PMID: 12821322

Abstract:

Recombinant Streptomyces griseus aminopeptidase (SGAP) was produced using Cangene's expression system, CANGENUS. This heat-stable aminopeptidase with an N-terminal Ala-Pro-Asp-Ile-Pro-Leu-Ala-Asn-Val-Lys-Ala sequence was purified from 16L of Streptomyces lividans fermentation supernatant with high purity and 19.5% recovery rate. This was achieved by the combination of hydrophobic-interaction and size-exclusion chromatographic procedures. The calcium-activated zinc metalloprotein demonstrated no loss of activity at -20 degrees C for at least 8 weeks in both liquid and freeze-dried formulations. The recombinant SGAP showed an apparent molecular mass of 31 kDa by sodium dodecyl sulfate/polyacrylamide gel electrophoresis and 26.8 kDa by gel filtration. The simple, high-yield, inexpensive purification method with few intermediate steps provides a novel and practical procedure for large-scale production of active recombinant S. griseus aminopeptidase.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9031941	Aminopeptidase I from Streptomyces griseus		9031-94-1	Price

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