title: Urease activity in microbiologically-induced calcite precipitation.
abstract: The role of microbial urease in calcite precipitation was studied utilizing a recombinant Escherichia coli HB101 containing a plasmid, pBU11, that encodes Bacillus pasteurii urease. The calcite precipitation by E. coli HB101 (pBU11) was significant although its precipitation level was not as high as that by B. pasteurii. Addition of low concentrations (5-100 microM) of nickel, the cofactor of urease, to the medium further enhanced calcite precipitation by E. coli (pBU11). Calcite precipitation induced by both B. pasteurii and E. coli (pBU11) was inhibited in the presence of a urease inhibitor, acetohydroxamic acid (AHA). These observations on the recombinant urease have confirmed that urease activity is essential for microbiologically-induced calcite precipitation. Partially purified B. pasteurii urease was immobilized in polyurethane (PU) foam to compare the efficacy of calcite precipitation between the free and immobilized enzymes. The immobilized urease showed higher K(m) and lower V(max) values, which were reflected by a slower overall calcite precipitation. However, scanning electron micrographs (SEM) identified that the calcite precipitation occurred throughout the matrices of polyurethane. Furthermore, PU-immobilized urease retained higher enzymatic activities at high temperatures and in the presence of a high concentration of pronase, indicating that immobilization protects the enzyme activity from environmental changes.
authors.affiliation: South Dakota School of Mines and Technology, Rapid City, SD 57701, USA.
authors.forename: Keri L
authors.initials: KL
authors.lastname: Bachmeier
authors.forename: Amy E
authors.initials: AE
authors.lastname: Williams
authors.forename: John R
authors.initials: JR
authors.lastname: Warmington
authors.forename: Sookie S
authors.initials: SS
authors.lastname: Bang
mesh_terms: D001407:Bacillus / Q000201:enzymology*; D002119:Calcium Carbonate / Q000378:metabolism*; D011232:Chemical Precipitation; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004800:Enzymes, Immobilized; D004926:Escherichia coli / Q000201:enzymology*; D006877:Hydroxamic Acids / Q000494:pharmacology; D007700:Kinetics; D008855:Microscopy, Electron, Scanning; D009532:Nickel / Q000494:pharmacology; D010957:Plasmids / Q000235:genetics; D011140:Polyurethanes; D011402:Pronase / Q000494:pharmacology; D011994:Recombinant Proteins / Q000378:metabolism; D013696:Temperature; D014510:Urease / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*
chemical_list: D004791:Enzyme Inhibitors; D004800:Enzymes, Immobilized; D006877:Hydroxamic Acids; D011140:Polyurethanes; D011994:Recombinant Proteins; C006358:acetohydroxamic acid; D009532:Nickel; D011402:Pronase; D014510:Urease; D002119:Calcium Carbonate