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. 2024 Oct 22;14:24266. doi: 10.1038/s41598-024-73955-y

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 4 — Expression, purification, and characterization of CPF_0394 (hyaluronate lyase CpeHysA). a halo assay for HA degradation using the cell extract obtained from the CpeHysA-expressing recombinant E. coli. Plates before (left) and after (right) addition of acetic acid. +, BL21-Gold(DE3)pLysS harboring pET21b-CPF_0394; and —, BL21-Gold(DE3)pLysS. b SDS-PAGE followed by CBB staining of the purified CpeHysA. Lane M, unstained marker of protein standard; lane P, purified CpeHysA. c Optimal pH. Buffers were sodium acetate (circle), potassium phosphate (triangle), Tris-HCl (square), and glycine-NaOH (rhombus). The activity measured in sodium acetate (pH 5.5) at 30 °C was taken as 100%. d Optimal temperature. The activity measured in Tris-HCl (pH 7.5) at 60 °C was taken as 100%. e Thermostability. The activity measured in Tris-HCl (pH 7.5) at 30 °C using CpeHysA preincubated at 45 °C was taken as 100%. f Substrate specificity. The activity measured in Tris-HCl (pH 7.5) at 30 °C using HA was taken as 100%. Each measurement represents the mean of three individual experiments.