Effects of anionic surfactants SDS and SDBS on the conformation and activity of bacterial collagenase

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Abstract Anionic surfactants are essential additives for leather-making, routinely employed on beamhouse processes in combination with industrial enzyme preparations. However, few studies have elaborated the effects of surfactants on bacterial collagenase—a harmful component in industrial enzyme preparations that degrade collagen and impair leather quality. Here, we investigated the effects of two anionic surfactants, sodium dodecyl sulfate (SDS) and sodium dodecyl benzene sulfonate (SDBS), on the activity of collagenase G (ColG), a representative bacterial collagenase. The results showed that both anionic surfactants could significantly inhibit the hydrolytic activity of ColG. In comparison with SDS, SDBS exhibited a stronger inhibitory effect on ColG at lower concentrations. Spectroscopy, molecular docking, and molecular dynamics simulation were employed to investigate the surfactant-bacterial collagenase interactions. The results indicated that both SDS and SDBS inhibited ColG primarily by occupying the active site of ColG and inducing conformational changes in the catalytic region. Compared with SDS, SDBS exhibited significantly higher binding affinity toward ColG and induced more pronounced conformational alterations of collagenase, resulting from π-conjugation effects and steric hindrance of its benzenesulfonate moiety. These findings not only facilitate optimized coordination between surfactants and industrial enzymes in leather-making processes but also provide theoretical support for developing bacterial collagenase inhibitors. Graphical Abstract

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