A Highly Active Chondroitin Sulfate Lyase ABC for Enzymatic Depolymerization of Chondroitin Sulfate

Abstract

Enzymatic preparation of low-molecular-weight chondroitin sulfate (LMWCS) has received increasing attention. In this work, a chondroitin sulfate lyase ABC (Chon-ABC) was successfully cloned, expressed, and characterized. The Km and Vmax of the Chon-ABC were 0.54 mM and 541.3 U mg−1, respectively. The maximal activity was assayed as 500.4 U mg−1 at 37 °C in pH 8.0 phosphate buffer saline. The half-lives of the Chon-ABC were 133 d and 127 min at 4 °C and 37 °C, respectively. Enzymatic preparation of LMWCS was performed at room temperature for 30 min. The changes between the substrate and product were analyzed with mass spectrometry (MS), high-performance liquid chromatography (HPLC), gel permeation chromatography (GPC), and nuclear magnetic resonance (NMR). Overall, the Chon-ABC from Bacteroides thetaiotaomicron is competitive in large-scale enzymatic preparation of LMWCS for its high activity, stability, and substrate specificity.

The efficacy and safety of condoliase for lumbar disc herniation: a systematic review and meta-analysis

“…The chondroitin sulfate ABC endolyase (condoliase) is a mucopolysaccharide enzyme. It is highly substrate-specific for chondroitin sulfate and hyaluronic acid ( Fan et al, 2022 ). Therefore, condoliase can specifically degrade proteoglycan-rich NP tissues, whereas the surrounding tissue remains largely unaffected ( Ishibashi et al, 2019 ).…”