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자료유형
학술저널
저자정보
Qing Liu (Pukyong National University) Shujing Sun (Qingdao Agricultural University) Meizi Piao (Qingdao Agricultural University) Ji Young Yang (Pukyong National University)
저널정보
한국식품영양과학회 Preventive Nutrition and Food Science Preventive Nutrition and Food Science Vol.18 No.4
발행연도
2013.12
수록면
273 - 279 (7page)

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Protease widely exists in the digestive tract of animals and humans, playing a very important role in protein digestion and absorption. In this study, a high protease-producing strain Planomicrobium sp. L-2 was isolated and identified from the digestive tract of Octopus variabilis. The strain was identified by physiological and biochemical experiments and 16S rDNA sequences analysis. A protease was obtained from the strain Planomicrobium sp. L-2 through ammonium sulfate precipitation, dialysis and enrichment, DEAE-Sephadex A50 anion-exchange chromatography, and Sephadex G-100 gel chromatography. The molecular weight and properties of the protease were characterized, including optimum temperature and pH, thermal stability, protease inhibitions and metal ions. According to our results, the protease from Planomicrobium sp. L-2 strain designated as F1-1 was obtained by three-step separation and purification from crude enzyme. The molecular weight of the protease was 61.4 kDa and its optimum temperature was 40℃. The protease F1-1 showed a broad pH profile for casein hydrolysis between 5.0∼11.0. No residual activity was observed after incubation for 40 min at 60℃ and 60 min at 50℃. F1-1 protease was inhibited by Mn<SUP>2+</SUP>, Hg<SUP>2+</SUP>, Pb<SUP>2+</SUP>, Zn<SUP>2+</SUP>, and Cu2+ ions, as well as PMSF, indicating that the protease F1-1 was a serine protease. Additionally, research basis provided by this study could be considered for industrial application of octopus intestinal proteases.

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ABSTRACT
INTRODUCTION
MATERIALS AND METHODS
RESULTS
DISCUSSION
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