Purification and characterization of β-agarase from Paenibacillus sp.

Mei, J., Tang, Z., Yi, Y., Wang, H., Wang, H., Wang, Q., and Ying, G. (2015). "Purification and characterization of β-agarase from Paenibacillus sp.", Food Science and Biotechnology, 23(5), pp. 1605-1609. doi : 10.1007/s10068-014-0218-x  Access to full text


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 50°C and the favorable agar-hydrolysis activity was at 40°C. 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{/sun} and maximal reaction velocity V max of purified agarase WL were 3.22 mg/mL and 41.5 μg/mL·min, respectively. The agarase WL was highly agar specific.

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