Abstract：
:cDNA coding a prolyl aminopeptidase (PAP) was cloned from Aspergillus oryzae and over expressed in Bacillus subtilis with a 6×His tag in N-terminus. The recombinant prolyl aminopeptidase was secreted to extracellular by adding 2 mM CaCl2 and 5% D-sorbitol in TB medium; the enzyme activity in fermented supernatant increased from 7.2 to 41.5 U mL-1. It has been purified 4.3-fold through Ni-chelating affinity chromatography with a recovery of 47.3%. The purified enzyme is stable below 50 °C and within pH 6-11, and with the highest activity at pH 7.5 and 50 °C. Several kinds of salt can activate enzyme activity in a certain concentration and the relative activity was 127.02% even when the concentration of NaCl reached 4.36 M. It cleaved N-terminal Pro residues from many peptides but shown different hydrolysis rates for various Pro-X dipeptides or peptides which are of different lengths. It combined with alkaline protease and leucine aminopeptidase to hydrolyze casein, many free amino acid especially proline and small peptide of hydrolysate increased significantly.
journal_name
Appl Biochem Biotechnoljournal_title
Applied biochemistry and biotechnologyauthors
Wang KD,Wang KH,Zhou ND,Tian YPdoi
10.1007/s12010-016-2305-3subject
Has Abstractpub_date
2017-04-01 00:00:00pages
1611-1623issue
4eissn
0273-2289issn
1559-0291pii
10.1007/s12010-016-2305-3journal_volume
181pub_type
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