Insufficient stability of proteins is a fundamental problem that restricts their application in the (bio)chemical industry. For example, low enzyme thermostability represents a frequently encountered yet unresolved limitation in the enzymatic synthesis of polymers and bio-diesels. Although different ways have been reported to increase protein thermostability, an approach that works for a specific protein may not always work for others. The herein presented research seeks to develop a general method to create protein thermostability. To this end, we utilize thermophilic maltose binding protein (ThMBP) as a universal scaffold into which a target protein is inserted. In our studies, we selected insertion sites of ThMBP based on our hypothesis that structural integrity of the scaffold protein ought to be maintained upon insertion of a target protein. Briefly, we first searched for sites of mesophilic maltose binding protein (MeMBP) where insertion or deletion of amino acid sequences generated no effect on the maltose binding affinity. We then identified the corresponding insertion sites of ThMBP through structural superposition between ThMBP and MeMBP. Subsequently, a model protein, beta-lactamase(BLA) was inserted into ThMBP sites by gene fusion. BLA activities of some of resultant proteins increased with increasing temperature up to 80 degree C. In contrast, the wild type BLA is not active above 50 degree C. Effect of temperature on BLA activities was reversible even after multiple temperature cycles. Effect of insertion site on BLA thermostability will be discussed and biophysical studies on this thermostability will be presented.