Characterization and Properties of a New Thermoactive and Thermostable Carbonic Anhydrase

被引:17
作者
Capasso, Clemente [1 ]
De Luca, Viviana [1 ]
Carginale, Vincenzo [1 ]
Caramuscio, Pompilio [3 ]
Cavalheiro, Catarina F. N. [3 ]
Cannio, Raffaele [4 ]
Rossi, Mose [1 ,2 ]
机构
[1] CNR, Ist Biochim Prot, Via P Castellino 111, I-80131 Naples, Italy
[2] Uni Fed II, Centro Ric Interdipartimentale Biomateriali, I-80125 Naples, Italy
[3] ENEL Ingn Innovazione SpA3, I-00198 Rome, Italy
[4] CNR, Ist Microelettron Microsistemi IMM, I-80131 Naples, Italy
来源
IBIC2012: INTERNATIONAL CONFERENCE ON INDUSTRIAL BIOTECHNOLOGY | 2012年 / 27卷
关键词
ESCHERICHIA-COLI; PURIFICATION; EXPRESSION; STABILITY;
D O I
10.3303/CET1227046
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
A new carbonic anhydrase was isolated and characterized from the thermophilic bacterium Sulfurihydrogenibium sp. YO3AOP1. The encoding gene was cloned and expressed in Escherichia coli and the recombinant protein purified to homogeneity. This enzyme (SspCA) belongs to the class of the carbonic anhydrase family, is a monomer of 26.1 kDa and shows esterase activity. The kinetic parameters were determined by using CO2 and p-nitrophenylacetate (p-NpA) as substrates. Thermoactivity and thermostability studies showed that SspCA is active in the temperature range from 0 to 100 degrees C and retains full activity after 2 h incubation at 100 degrees C. SspCA was immobilized within a polyurethane foam and was found to be unalterably active and stable up to 50 h at 100 degrees C.
引用
收藏
页码:271 / 276
页数:6
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