Production and purification of sarcosine oxidase (SOx) in <i>Escherichia coli</i> was analyzed and optimized in order to maximize SOx functionality and affordability for the design of a sarcosine biosensor. Sarcosine oxidase catalyzes the oxidative demethylation of sarcosine, a potential biomarker for early stage prostate cancer. Sarcosine levels can be detected via amperometry measuring the hydrogen peroxide by-product of the enzymatic reaction at an electrode modified with immobilized SOx. Developing a non-invasive, highly specific amperometric sarcosine biosensor with high sensitivity has significant implications for prostate cancer detection and diagnosis. In order to circumvent the cost-prohibitive purchase of SOx, we developed a procedure to synthesize the enzyme to a level of equivalent purity and activity to SOx purchased from vendors. This procedure is a cost-effective and efficient way to produce large quantities of enzyme, thus providing the opportunity to further investigate the optimal ways to solubilize, stabilize, and immobilize SOx for use in sarcosine biosensing systems. Examples of SOx-based biosensors are presented.

Optimization of sarcosine oxidase isolation and purification for use in amperometric biosensors

253rd National Meeting (2017)

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