Advancing the analysis of terbutaline in urine samples using novel enzyme hydrolysis

Abstract

Aim: To investigate the efficiency of two new fast-acting enzymes, recombinant arylsulfatase (IMCS-PSF) and mutant β-glucuronidase from Escherichia coli (IMCSzyme), in hydrolyzing specific terbutaline metabolites. Materials & methods: Two purified novel enzymes are used to precisely determine the amount of each metabolite in urine at different time points after oral administration. After systematically evaluating the hydrolysis efficiency of the novel enzymes compared with commercially available enzymes, these recently developed enzymes were applied to establish the separate urine concentration profiles of terbutaline and each metabolite. Results & discussion: The results highlight the highly efficient arylsulfatase enzyme expressed from E. coli for urine analysis of terbutaline while suggesting sulfoconjugates as the main terbutaline metabolites. Conclusion: This study demonstrated the high efficiency of the IMCS-PSF enzyme in hydrolyzing terbutaline conjugates in comparison with other enzyme reagents typically used for the analysis of terbutaline and sulfoconjugates are the main terbutaline metabolites in urine.