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. 2024 Nov 22;24(6):5. doi: 10.1093/jisesa/ieae101

Fig. 7.

Graphs labeled A-D illustrate the results of the purification of Cellulase-28a and GcEGaseZ7-28a. A depicts the SDS-PAGE analysis of the broken Cellulase-28a bacterial liquid. B presents SDS-PAGE analysis of purified Cellulase-28a. C depicts SDS-PAGE analysis of broken GcEGaseZ7-28a bacterial liquid. D is SDS-PAGE analysis of purified GcEGaseZ7-28a.

Purification of Cellulase-28a and GcEGaseZ7-28a. Note: M: Molecular weight of protein marker, size marked on the left; A) 1–2: Uninduced and induced expression bacteria of Cellulase-28a; 3–4: The fragmented supernatant of Cellulase-28a; 5–8: Undiluted, 5-fold dilution, 10-fold dilution, and 20-fold dilution of Cellulase-28a precipitates after fragmentation; 9–11: 0.2 mg/ml, 0.3 mg/ml, and 0.4 mg/ml of BSA. B) 1–4: Undiluted, 5-fold dilution, 10-fold dilution, and 20-fold dilution of Cellulase-28a dissolved in 8M urea and precipitated after fragmentation; 5–6: 0.2 mg/ml and 0.4 mg/ml of BSA. C) 1–3: Untreated, the supernatant of GcEGaseZ7-28a purified by His tag and the eluate of the supernatant of GcEGaseZ7-28a fragmented and purified by His tag; 4–7: Untreated, 5-fold dilution, 10-fold dilution, and 20-fold dilution after dialysis and concentration of the eluted protein obtained from the supernatant of GcEGaseZ7-28a purified by His tag; 8–10: 5-fold dilution, 10-fold dilution, and 20-fold dilution of GcEGaseZ7-28a precipitates after fragmentation; 11–13: 0.2 mg/ml, 0.3 mg/ml, and 0.4 mg/ml BSA. D) 1–3: 5-fold dilution, 10-fold dilution, and 20-fold dilution of GcEGaseZ7-28a dissolved in 8M urea and precipitated after fragmentation; 4–6: 0.2 mg/ml 0.3 mg/ml and 0.4 mg/ml BSA.