Enhancing the thermostability of a mono- and diacylglycerol lipase from Malassizia globose by stabilizing a flexible loop in the catalytic pocket

•A library of variants was built using error-prone PCR for a diacylglycerol lipase.•Thousands of variants were screened to identify multiple stabilized mutants.•Thermostability and enzymatic activity were both improved for a double mutant.•Unfolding MD-simulation revealed mechanisms of thermostability enhancement.