|
KMID : 1160620130180040273
|
|
Preventive Nutrition and Food Science
2013 Volume.18 No. 4 p.273 ~ p.279
|
|
|
Purification and Characterization of a Protease Produced by a Planomicrobium sp. L-2 from Gut of Octopus vulgaris
|
|
Liu Qing
Sun Shujing
Piao Meizi
Yang Ji-Young
|
|
|
Abstract
|
|
|
|
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 identi-fied 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 40oC. 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 60oC and 60 min at 50oC. F1-1 protease was inhibited by Mn2+, Hg2+, Pb2+, Zn2+, 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.
|
|
|
KEYWORD
|
|
|
enzymatic properties, identification, intestinal bacteria, octopus, purification
|
|
|
FullTexts / Linksout information
|
|
|
|
|
Listed journal information
|
|
|
|