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Novel protein engineering of lipase by protein folding memory (567.1)

Some hydrolytic enzymes including lipases and proteases have propeptides in their N‐ or C‐ terminals. Such propeptides seem to function as an intramolecular chaperone to facilitate the folding of their active domain and are cleaved off after completion of the function as chaperone. By introducing mutations into propeptides of lipases and altering the chaperone functions, we have successfully created altered lipases which showed improved activities and stabilities, in spite of the same primary sequences as the original lipase. We named this phenomenon “protein folding memory”, because mutations in the propeptide imprinted memories into the mature enzyme structures [1]. Our study aimed to alter a substrate recognition of Rhizopus oryzae lipase (ROL) by protein folding memory. Eight hydrophilic amino‐acids were introduced into a part of the propeptide essential for the folding of ROL. This propeptide‐mutated ROL showed a 1.3‐fold higher lipase activity than that of WT ROL. In addition, the propeptide‐mutated ROL remarkably exhibited a peptidase activity, which was absent in the original form [2]. Here, we report the structural and functional differences between WT ROL and propeptide‐altered ROL with the same primary sequence.