Nagoya, Japan

Chie Idekoba


Average Co-Inventor Count = 9.0

ph-index = 1

Forward Citations = 6(Granted Patents)


Company Filing History:


Years Active: 1996-1997

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2 patents (USPTO):Explore Patents

Title: Chie Idekoba: Innovator in Protein Disulfide Isomerase Technology

Introduction

Chie Idekoba is a prominent inventor based in Nagoya, Japan. She has made significant contributions to the field of biochemistry, particularly in the development of highly thermostable polypeptides with protein disulfide isomerase (PDI) activity. With a total of 2 patents, her work is paving the way for advancements in protein refolding processes.

Latest Patents

Chie Idekoba's latest patents focus on polypeptides possessing protein disulfide isomerase activity. The first patent describes a highly thermostable polypeptide characterized by its ability to catalyze disulfide exchanges in proteins. This polypeptide recognizes ribonuclease A as a substrate and operates effectively at temperatures ranging from 20 to 70 degrees Celsius. It remains stable at a pH value of 6 to 9 and has a molecular weight of approximately 60,000 to 62,000. The enhanced thermostability and stable activity across a broader dithiothreitol concentration range make this enzyme particularly useful for refolding certain proteins. The second patent similarly outlines a polypeptide from Humicola insolens, emphasizing its production process using transformed expression vectors.

Career Highlights

Chie Idekoba is associated with Kabushiki Kaisha Toyota Chuo Kenkyusho, where she continues to innovate in her field. Her work has garnered attention for its potential applications in various biotechnological processes.

Collaborations

Chie collaborates with notable colleagues, including Yukio Yamada and Osamu Asami, who contribute to her research endeavors.

Conclusion

Chie Idekoba's innovative work in the field of protein disulfide isomerase technology showcases her dedication to advancing biochemistry. Her patents reflect a commitment to developing solutions that enhance protein refolding processes, marking her as a significant figure in her field.

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