|
KMID : 1007520140230051605
|
|
Food Science and Biotechnology
2014 Volume.23 No. 5 p.1605 ~ p.1609
|
|
|
Purification and Characterization of β-Agarase from Paenibacillus sp.
|
|
Mei Jianfeng
Tang Zhongxiu
Yi Yu
Wang Hong
Wang Qi
Ying Guoqing
|
|
|
Abstract
|
|
|
|
β-Agarase produced by Paenibacillus sp. WL (agarase WL) was purified using a combination of ammonium sulfate precipitation, DEAE-ion exchange, and gel-filtration chromatography. The purity of the agarase was increased by 11.9× with a recovery of 5.1% and a specific activity of 4,670.1 U/mg of protein. The molecular mass of the purified agarase was approximately 30 kDa (SDS-PAGE). The agarase was stable at temperature below 50oC and the favorable agar-hydrolysis activity was at 40oC. The agarase was active in the range of pH 5.0 to 8.0, and the optimal agar-hydrolysis pH value was approximately 6.0. Metal ions normally found in seawater (Na+, K+, Ca2+, Mg2+, and Al3+) could activate agarase WL. The Michaelis-Menten constant Km and maximal reaction velocity Vmax of purified agarase WL were 3.22 mg/mL and 41.5 μg/mL·min, respectively. The agarase WL was highly agar specific.
|
|
|
KEYWORD
|
|
|
agarase, Paenibacillus sp, purification, enzymatic characteristics
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
 
|