Marine urease with higher thermostability, pH and salinity tolerance from marine sponge-derived Penicillium steckii S4-4
- PDF / 1,712,362 Bytes
- 8 Pages / 595.276 x 790.866 pts Page_size
- 115 Downloads / 152 Views
RESEARCH PAPER
Marine urease with higher thermostability, pH and salinity tolerance from marine sponge‑derived Penicillium steckii S4‑4 Changrong Liu1 · Yao Xiao1 · Yilin Xiao1 · Zhiyong Li1 Received: 7 March 2020 / Accepted: 16 September 2020 © Ocean University of China 2020
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 p rotein−1. The molecular weight of the enzyme was 183 kDa and a single subunit of 47 kDa 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 Km of 7.3 mmol L−1 and a Vmax of 1.8 mmol urea m in−1 mg 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 30 min, pH 5.5–10.0 or 0–25% salinity for 6 h. 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. Keywords Marine urease · Penicillium steckii · Thermostability · Alkali resistance · Salinity tolerance
Introduction Urease (urea amidohydrolase, EC 3.5.1.5) as the first enzyme crystallized from Jack bean and the first enzymatic protein possessing nickel ions in the active site (Dixon et al. 1975), hydrolyzes urea to yield ammonia and carbamate. To date, urease has been found widespread in organisms including archaea (Bhatnagar et al. 1984), cyanobacteria (Carvajal et al. 1982; Collier et al. 1999; Palinska et al. 2000; Rai 1989), bacteria (Benoit and Maier 2011; Cai and Ni 1996; Liu et al. 2017a; Todd and Hausinger 1987; Turbett et al. 1992), fungi (Geweely 2006; Jahns 1995; Lubbers et al. 1996; Mirbod et al. 2002), plants (Das et al. 2002; Edited by Chengchao Chen. * Zhiyong Li [email protected] 1
Marine Biotechnology Laboratory, State Key Laboratory of Microbial Metabolism, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, China
El-Hefnawy et al. 2014; Hirayama et al. 2000; Menegassi et al. 2008) and invertebrates (Mcdonald et al. 1980). Urease has been well used in determining the concentration of blood urea in clinical diagnosis (Qin and Cabral 2002), removing the urea lest forming carcinogenic ethyl carbamate in alcoholic beverages (Yang et al. 2015), detecting heavy metal ion pollutants in environmental protecti
Data Loading...
