Multifunctional enzyme, which shows esterase and perhydrolase activities, and is capable of organic acid-assisted bromination of organic compounds (PubMed:10601844, PubMed:12542698). Catalyzes the hydrolysis of 3,4-dihydrocoumarin (PubMed:10601844, PubMed:12542698). Aromatic lactones other than 3,4-dihydrocoumarin, such as 2-coumaranone and homogentisic acid lactone, are also substrates, but their activities relative to that of 3,4-dihydrocoumarin are quite low (PubMed:10601844). Also catalyzes the hydrolysis of several linear esters, with specificity toward methyl esters (PubMed:12436309). In addition, shows perhydrolase activity and catalyzes the dose- and time-dependent degradation of peracetic acid, a broad-spectrum biocide, to acetic acid and hydrogen peroxide (PubMed:12542698). It suggests that in vivo DCH may play a role in the oxidative stress defense system and detoxify peroxoacids in conjunction with the catalase, i.e. peroxoacids are first hydrolyzed to the corresponding acids and hydrogen peroxide by DCH, and then the resulting hydrogen peroxide is degraded by the catalase (PubMed:12542698). Also shows organic acid-assisted bromination activity toward monochlorodimedon when incubated with hydrogen peroxide and dihydrocoumarin or an organic acid, such as acetate and n-butyrate (PubMed:10601844, PubMed:12542698). 3,4-dihydrocoumarin + H2O = 3-(2-hydroxyphenyl)propanoate + H(+) H2O + peracetic acid = acetate + H(+) + H2O2 a percarboxylic acid + H2O = a carboxylate + H(+) + H2O2 Inhibited by the serine protease inhibitors diisopropyl fluorophosphate and phenylmethanesulfonyl fluoride. Optimum pH is 7.0-8.0. Optimum temperature is 30 degrees Celsius. Stable below 75 degrees Celsius, and retains 69% of the original activity at 80 degrees Celsius. Homodimer. Disruption mutant is more sensitive to growth inhibition by peracetic acid than the parent strain. The sensitivities to hydrogen peroxide and acetic acid are not affected. Can convert substrates at high concentrations to desirable products in a short time. Thus, DCH exhibits significant hydrolysis activity, with stereo and/or regioselectivity, toward the methyl esters of bacetylthioisobutyrate and cetraxate, and is expected to be applicable to the practical synthesis of these compounds. Belongs to the AB hydrolase superfamily. Bacterial non-heme haloperoxidase / perhydrolase family.