들깨잎 폴리페놀 산화효소의 Ph 및 온도에 의한 영향

• 영문명: Influence of Ph and Temperature on Polyphenol Oxidase in the Leaves of Perilla frutescens var. japonica
• 발행기관: 대한약학회
• 저자명: 김유경(Yoo Kyung Kim) 김안근(An Keun Kim)
• 간행물 정보: 『약학회지』제48권 제6호 (2004년), 384~390쪽, 전체 7쪽
• 주제분류: 의약학 > 기타의약학
• 파일형태: PDF
• 발행일자: 2004.12.31

영문 초록

Polyphenol oxidase-catalyzed oxidation of substrates (t-butylcatechol, 4 methylcatechol, chlorogenic acid, caffeic acid and pyrocatechol) were performed in the Ph range 4~8. Concentrations of substrate's major oxidation products were monitored by high performance liquid chromatograph. The nature and amounts of products formed were highly pH dependent. They also were ifluenced by kinds of substrates. Major oxidation product of 4-methylcatechol appeared the maxium value at pH 5, them of chlorogenic acid, caffeic acid and pyrocatechol at pH 6.0 and that of t-butylcatechol at pH 5~7. Time-dependent PPO activity was determined at 4℃ and 30℃. PPO extracted by phosphate buffer containing triton X-114 (t-PPO) was more stable than PPO by phosphate buffer (b-PPO). The result of electrophoresis, at first PPO was showed only a band at 48 kd. After 1~3 days a partial degrade band was appeared in b-PPO and three partial degrade bands in t-PPO. No activity band was appeared in PPOs at 30℃ and b-PPO at 4℃ after 4 days. And a band (37 kDa) in t-PPO was remained finally and disappered. PPO from Perillae leaves has two activity bands at 48 and 37 kDa in previous paper. It was supposed that PPO in the leaves of Perilla frutescens was a protein having one molecular weight as 48 kDa. And 37 kDa protein, relatively proteolysis-resistant, was a proteolyzed form of a major form.

키워드

polyphenol oxidase pH temperature