Bioinformatics analysis of schwanniomyces occidentalis alpha amylase secretion signal sequences

The amy gene from schwaniomyces occidentalis which encodes a secretory alpha amylase isolated by primers that designed from sequences derived from Gene bank. The isolated gene is then cloned into a p426gpd vector. After cloning, the recombinant vector was transformed into E.Coli DH5x strain and recombinant vector was sent for sequencing by T7, T3 and a mid primer. After sequencing, the sequence of the alpha amylase gene is then converted to amino acid sequence and the new hypothetical protein was analyzed by several signal peptide analysis programs. The cleavage sites and intracellular localization of the protein inside the cell is detected by this analysis. The results showed that schwanniomyces occidentalis alpha amylase has a 25 amino acid long secretory signal peptide that is responsible for initiation of transportation of the enzyme across endoplasmic reticulum, through the secretory pathway and finally secretion out of the cell. Our result would prove very important not only for production of these enzymes but also protein analysis and creating the recombinant organism that produce these enzymes.