Purification and Properties of Apple Pectinesterase

✍ Scribed by Macdonald, Helen M.; Evans, Roger

• Publisher: John Wiley and Sons
• Year: 1996
• Tongue: English
• Weight: 484 KB
• Volume: 70
• Category: Article
• ISSN: 0022-5142
• DOI: 10.1002/(sici)1097-0010(199603)70:3<321::aid-jsfa505>3.0.co;2-9

✦ Synopsis

Pectinesterase from apple was separated into two fractions by chromatography on Sephadex G-75. The major pectinesterase was purified by cationexchange chromatography on CM-Sephadex C-50. It had a molecular mass of 36 kDa, and isoelectric point of about 9, similar to one of the major pectinesterases of lemon. The enzyme required the presence of cations for optimum activity and was completely inactive at temperatures above 75°C. Although the major pectinesterase had no effect on the cloud stability of apple juice, a fraction containing a minor pectinesterase caused cloud clarification.