Development of a New Method to Analyze the Procof Protein Thermal Inactivation: A Design Guideline for Protein Thermostabilization
September 28(Thu), 2017
The research group led by Associate Professor Junichiro Futami of Okayama University Graduate School of Natural Science and Technology (Department of Medical Bioengineering) has developed a new method to analyze the “starting point” of the irreversible thermal denaturation/inactivation of protein. This research result was published in the British scientific journal Scientific Reports on September 29.
Proteins have 20 types of amino acids and is a versatile material that forms an ordered three-dimensional structure to express various biological functions. Proteins use disulfide (SS) bonds, in which side chains of amino acids called cysteines are cross-linked, as “pillars” in order to form and maintain the highly- ordered three-dimensional structure. Heating protein results in a denatured state where the three-dimensional structure is destroyed. However, as long as the “pillars” are intact, many of the proteins can refold into their native three-dimensional structure after cooling. The research group of Associate Professor Futami took notice of the mechanism whereby heat-induced SS bond breakages inside protein molecules set off a SS-shuffling chain-reaction of protein unfolding. The group discovered that the irreversible heat-inactivation of proteins can be greatly suppressed by adding methanethiosulfonate type reagents that quickly eliminate thiol and perthiol groups, which are the starting point of the reaction.
By utilizing this research method, we can explore the weaknesses of heat inactivation of individual proteins and obtain important information that will help us to improve the thermostabilization of proteins beneficial for industrial use.
Journal: Scientific Reports
Title: Evaluation of irreversible protein thermal inactivation caused by breakage of disulphide bonds using methanethiosulphonate
Authors: Junichiro Futami, Ai Miyamoto, Atsushi Hagimoto, Shigeyuki Suzuki, Midori Futami & Hiroko Tada
Year of Publication: 2017
Okayama University Silicon Valley Office (OUSVO)
Contact: Mototaka Senda, Ph.D.
- protein thermal, methanethiosulphonate, amino acids