THE PROSPECT OF USING BAKERDREAM YEAST (SACCHAROMYCES CEREVISIAE) IN THE PRODUCTION O ENZYMES

Abstract

The oligopeptide was isolated, purified and the amino acid composition was studied from the yeast Saccharomyces cerevisiae. Using the data obtained, enzymes were analyzed from the database closer in terms of molecular weight and analysis of the amino acid composition of the resulting oligopeptide. Among the enzymes of the Saccharomyces cerevisiae strain S288C, the most convenient enzymes for preparing the conjugate for ELISA are PHO3, PHO5, PHM8, PHO11, PHO12, putative acid phosphatase DIA3, PAH. phosphatidate phosphatase, glucan-1.3-beta-glucosidase EXG1, glutathione peroxidase URE2, cytochrome c peroxidase LPP1, GTT1, T-protein catalase CTT1. GPP1 has the lowest MolProbity and Clash scores, indicating slightly better structural quality. PHM8 and CPP1 have the highest number of lysine residues, which may offer more sites for conjugation compared to GTT1 and LPP1. GTT1 has the lowest collision score and MolProbity, indicating fewer steric clashes and potentially higher structural fidelity. PHM8: Contains a large number of lysine residues and good structural integrity, making it suitable for stable conjugation with BSA. This can improve stability, solubility and prolong half-life, which is useful for applications such as drug delivery and therapy. CCP1 is also a strong candidate with slightly more lysines and better structural quality, but its structural score is slightly higher than PHM8.