Study on the Interaction of a Cysteine Protease and Its Inhibitor from Sesame Seed

• Main Authors: Ramadhani Mahendra Kusuma, 馬漢德
• Other Authors: Douglas J. H. Shyu
• Format: Others
• Language: en_US
• Published: 2017
• Online Access: http://ndltd.ncl.edu.tw/handle/6rtxwh

碩士 === 國立屏東科技大學 === 生物科技系所 === 106 === Papain-like cysteine protease has been widely used worldwide and has been known to have a specific relationship with cystatin. To study the interactions between cysteine protease and cystatin, soluble fraction of recombinant cysteine protease expressed in Escherichia coli cloned from germinating sesame seed (SiCP) was purified using immobilized-cystatins coupled to sepharose affinity column. Purified-SiCP demonstrates a very similar proteolytic activity compared with papain toward substrate and decisively inhibited by SiCYS. SiCP enzymatic activity was found to be optimum at a slightly acidic pH and stable throughout a wide range of temperature ranged from 30 to 70 oC.