Marine urease with higher thermostability, pH and salinity tolerance from marine sponge-derived Penicillium steckii S4-4.

Abstract

Urease has a broad range of applications, however, the current studies on urease mainly focus on terrestrial plants or microbes. Thus, it is quite necessary to determine if marine-derived ureases have different characteristics from terrestrial origins since the finding of ureases with superior performance is of industrial interest. In this study, the marine urease produced by Penicillium steckii S4-4 derived from marine sponge Siphonochalina sp. was investigated. This marine urease exhibited a maximum specific activity of 1542.2 U mg protein-1. The molecular weight of the enzyme was 183kDa and a single subunit of 47kDa was detected, indicating that it was a tetramer. The N-terminal amino acid sequence of the urease was arranged as GPVLKKTKAAAV with greatest similarity to that from marine algae Ectocarpus siliculosus. This urease exhibited a K m of 7.3mmolL-1 and a V max of 1.8mmol urea min-1mg protein-1. The optimum temperature, pH and salinity are 55℃, 8.5 and 10%, respectively. This urease was stable and more than 80% of its maximum specific activity was detected after incubating at 25-60℃ for 30min, pH 5.5-10.0 or 0-25% salinity for 6h. Compared with the terrestrial urease from Jack bean, this marine urease shows higher thermostability, alkaline preference and salinity tolerance, which extends the potential application fields of urease to a great extent.