Abstract:

Proteases produced from Actinomucor elegans ( A. elegans) are of preferable debittering effect and high hydrolysis ability to soybean proteins. In order to reveal the relationship between the structure and the function and accelerate the development and application of the proteases,serine protease ( SP1) gene from A. elegans was obtained by means of PCR and RACE techniques,and was then predicted and analyzed in detail based on the bioinformatics theory and technology. The results show that SP1 gene,which contains 4 exons and 3 introns,encodes 454 amino acid residues, and that SP1 belongs to Proteinase K family and exhibits the closest genetic relationship to Rhizopus microsporus var. chinensis with the highest homology. Moreover,according to the SP1 structure modeled via homology modeling with Proteinase K ( PDB code: 1IC6) as the crystal coordinate,it is found that SP1 has no disulfide bonds and possesses a Ca^{2 +} binding site,and that the differences in substrate-binding region, hydrogen bond, salt bridge and disulfide bond between SP1 and Proteinase K are probably responsible for the special hydrolysis ability and debittering effect of SPI.

Key words: Actinomucor elegans, serine protease, gene cloning, sequence analysis