Development of a technology to degrade, remove or process persistent proteins with enzymes

2014 Fiscal Year Final Research Report

• Project/Area Number: 24380055
• Research Category: Grant-in-Aid for Scientific Research (B)
• Allocation Type: Partial Multi-year Fund
• Section: 一般
• Research Field: Applied biochemistry
• Research Institution: Osaka University
• Principal Investigator: KANAYA SHIGENORI 大阪大学, 工学(系)研究科(研究院), 教授 (30273585)
• Co-Investigator(Renkei-kenkyūsha): KOGA Yuichi 大阪大学, 大学院工学研究科, 准教授 (30379119) ; CLEMENT Angkawidjaja 大阪大学, 大学院工学研究科, 特任助教 (20505987) ; KANAYA Eiko 大阪大学, 大学院工学研究科, 特任研究員 (80396217)
• Project Period (FY): 2012-04-01 – 2015-03-31
• Keywords: クチナーゼ / ポリエステル / サチライシン / プリオン / カルシウム結合部位 / メタゲノム / Ｘ線結晶構造解析 / セルラーゼ

Outline of Final Research Achievements

The crystal structure of LC-cutinase with PET-degrading activity was determined. Then, the mutations were introduced into LC-cutinase and two proteases (Tk-subtilisin and Tk-SP) with abnormal prion-degrading activity based on their structures to improve their enzymatic properties. As a result, the LC-cutinase derivative with enhanced stability, the Tk-subtilisin derivative with increased maturation rate, and the Tk-SP derivative with high stability in the presence of EDTA were constructed. In addition, two thermostable cellulases were isolated from leaf-branch compost by a metagenomic approach and their crystal structures were determined.

Free Research Field

生化学