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Background  As an environmental pollutant, 4-hydroxyphenylacetate (4-HPA) was a product of softwood lignin decomposition and was found in industrial effluents from olive oil production.  Sulfobacillus acidophilus  TPY was a moderately thermoacidophilic bacterium capable of degrading aromatic compounds including 4-HPA. The enzymes involved in the degradation of 4-HPA and the role of this strain in the bioremediation of marine pollutants need to be illustrated.    Results  3,4-dihydroxyphenylacetate dioxygenase (DHPAO) encoded by  mhpB2  and two components of 4-hydroxydroxyphenylacetate (4-HPA) 3-hydroxylase encoded by  hpaB  and  hpaC  from  S. acidophilus  TPY, a moderately thermoacidophilic bacterium, involved in the degradation of 4-HPA possessed quite low amino acid sequence identity (22–53%) with other ever reported corresponding enzymes, which suggest their novelty. These two enzymes were expressed in  E. coli  and purified to homogeneity. DHPAO activity in  E. coli  was revealed by spraying with catechol or 3,4-dihydroxyphenylacetate (3,4-DHPA) on the colonies to make them turn brilliant yellow color. DHPAO possessed total activity of 7.81 U and 185.95 U/mg specific activity at the first minute when 3,4-DHPA was served as substrate. DHPAO was a thermophilic enzyme with optimum temperature of 50 °C and optimum substrate of 3,4-DHPA. The small component (HpaC) was a flavoprotein, and both HpaB and HpaC of 4-HPA 3-hydroxylase were NADH-dependent and essential in the conversion of 4-HPA to 3,4-DHPA. 4-HPA 3-hydroxylase possessed 3.59 U total activity and 27.37 U/mg specific activity at the first minute when enzymatic coupled assay with DHPAO was applied in the enzymatic determination.    Conclusions  The ability of this extreme environmental marine strain to degrade catechol and substituted catechols suggest its applications in the bioremediation of catechol and substituted catechols polluted marine environments.    Electronic supplementary material  The online version of this article (10.1186/s12866-019-1415-9) contains supplementary material, which is available to authorized users.

bmc microbiology

Characterization of enzymatic properties of two novel enzymes, 3,4-dihydroxyphenylacetate dioxygenase and 4-hydroxyphenylacetate 3-hydroxylase, from Sulfobacillus acidophilus TPY