Earticle

초록

영어

Polyphenoloxidase (PPO) was extracted from Solanum tuberosum Jasim by various chromatographic methods and was subsequently purified and characterized. PPO was purified upto 78-fold from the crude extract. SDS-PAGE profile of the enzyme showed a major subunit of PPO with molecular weight of 40 kDa. The optimum pH and temperature for the maximum activity of PPO was 6.5 and 25℃, respectively. The enzyme was found to be quite stable between 10 and 40℃, whereas it was almost inactivated at 70℃ when incubated for 30 min. Substrate specificity study indicated that catechol was the most suitable substrate for PPO isolated from purple-fleshed potato with a Km value of 21.1 mM. The most effective inhibitor was ascorbic acid, followed by L-cysteine, citric acid, EDTA, and boric acid. Studies on the effect of metal ion on PPO activity showed that magnesium and copper were inhibitory, while iron and zinc ions increased the activity of PPO.

목차

Abstract
 Introduction
 Materials and Methods
 Results and Discussion
 References

키워드

저자

• Jang, Jae-Won [ Department of Food Science and Technology, College of Agriculture and Life Sciences, Chungnam National University ]
• Ma, Yu-Hyun [ Department of Food Science and Technology, College of Agriculture and Life Sciences, Chungnam National University ]
• Shin, Ju-Mi [ Department of Food Science and Technology, College of Agriculture and Life Sciences, Chungnam National University ]
• Song, Kyung-Bin [ Department of Food Science and Technology, College of Agriculture and Life Sciences, Chungnam National University ] Corresponding author

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  Food Science and Biotechnology

• 간기

  격월간

• pISSN

  1226-7708

• 수록기간

  1992~2009

• 십진분류

  KDC 574 DDC 664