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Abstract
Identifying the active proteoforms of bioconversion enzymes from microbial sources is important for novel compound delivery in pharmaceutical companies. Many of these enzymes are heavily post-translational modified and the modifications are known to regulate the enzymatic activities. Our preliminary glycol-proteomics results suggest that Amylogucosidase in A. niger secretome is heavily glycosylated with both N-linked and O-linked glycans. Here, using Amyloglucisidase as the model system, we develop an integrated proteomics approach to correlate the enzymatic activity with its differently post-translational modified proteoforms. Various LC separation formats (e.g., ion exchange, size exclusive column) are selected to fractionate the total Amyloglucisidase extract. After evaluating the enzyme activities using glucose assay kits, the fractions containing the active proteoforms are further analyzed using the integrated top-down and bottom-up approach employed on an LTQ Orbitrap Velos mass spectrometry. The optimized method will be then applied to analyze the Amyloglucisidase in A. niger growing under different conditions (e.g., various pHs and temperatures).
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