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Home > Archive>Volume 35, Issue 1, 2016 >95-100. DOI:10.3969/j.issn.1673-1689.2016.01.015
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Structural Analysis of Acid Protease ( Ap) from Aspergillus oryzae
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    Abstract:

    Compared with some commercial proteases，acid protease（Ap） from Aspergillus oryzae has high hydrolysis efficiency and produces soy hydrosates with weaker bitterness. In order to uncover the structural characteristics，Ap gene from A. oryzae was cloned by RT-PCR technology，and then was analyzed with bioinformatics technology. Results showed that Ap gene had a preference for codon usage，especially for the third codon with the 74% usage frequency of GC base，and encoded 404 amino acid residues. Ap was an extracellular aspartic proteinase. According to the structure obtained by homology modeling with acid protease from A. phoenicis（PDB code：1IBQ），Ap was found to possess at least two Zn2+ binding sites，one disulfide bond，163 hydrogen bonds，35 salt bonds，and two solvent accessible surfaces of D33（4.7849?魡2） and D215（3.5941?魡2）. Though the spatial structures of Ap and 1IBQ were similar，residues of some important sites（such as flap ring，angle and ψ-loops） were conservative.

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KE Ye, LI Jiasheng, ZENG Songrong, ZHU Zhaojing. Structural Analysis of Acid Protease ( Ap) from Aspergillus oryzae[J]. Journal of Food Science and Biotechnology,2016,35(1):95-100.

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  • Online: March 11,2016
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