Reflectin proteins found in the Bragg lamellae of iridocyte cells mediate remarkable color-changing abilities of cephalopods. Neutralization of cationic linkers via neuronally activated phosphorylation cause reflectins to assemble into protein condensates. This creates an osmotic gradient, leading water to be ejected from the membranes and causing shrinkage. The shrinking and expanding of these membranes enables cephalopods to alter wavelengths of light reflected from their skin. Studying the structure and function of different proteins responsible for this phenomenon can teach us how to create and manipulate tunable biophotonic materials. For such studies, an abundant source of pure proteins are necessary. Previously, purifications of reflectin protein took about a month to complete. For optimization, our group developed a new protocol that reduces the purification time to 9 days. Time was cut down by eliminating a step from the previous chromatographic procedure and taking advantage of the recently acquired advanced instrumentation available in the campus’s shared BioPacific facility. This eliminated more than 15 days from the procedure, while allowing purification of nearly 30-fold more protein in each batch. When compared to the longer process, this method has successfully produced a higher yield and purity of reflectin A protein, the most studied reflectin. However, it has not been applied to reflectin B and C yet, two proteins more abundant in tunable cells which have yet to be fully studied. To support future studies, my project focused on utilizing the new protocol for reflectin C, achieving yields and purity comparable to those of reflectin A. We plan to use these purified proteins in biomimetic vesicles to examine their function and membrane-altering effects. Further improvements to the protocol may still be possible to enhance time efficiency in reflectin production.