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Ecological Function of Myroilysin, a Novel Bacterial M12 Metalloprotease with Elastinolytic Activity and a Synergistic Role in Collagen Hydrolysis, in Biodegradation of Deep-Sea High-Molecular-Weight Organic Nitrogen
Appl. Environ. Microbiol. Chen et al. 75: 1838
Supplemental material
Files in this Data Supplement:
- Supplemental file 1 - Purification of the protease secreted by Myroides profundi D25 (Table S1); purification of myroilysin by ion-exchange chromatography on a DEAE-Sepharose fast-flow column (Fig. S1); analysis of the purity of myroilysin by SDS-PAGE (Fig. S2); molecular mass of myroilysin determined by MALDI-TOF MS (Fig. S3); analysis of the present form of myroilysin by gel filtration chromatography using HPLC and FPLC (Fig. S4); thermal induced unfolding of myroilysin detected by a circular dichroism spectropolarimeter at 222 nm (Fig. S5); nucleotide and deduced amino acid sequences of myroilysin and schematic diagram of the deduced amino acid sequence of myroilysin (Fig. S6); degradation of fibrin and fibrinogen by myroilysin and pseudolysin (Fig. S7); analysis of the hydrolytic products of oxidized insulin B chain by myroilysin (Fig. S8); spectrum of the products of oxidized insulin B chain hydrolyzed by myroilysin (Fig. S9); MS spectra of peptides 1 to 7 (Fig. S10); determined molecular masses and sequences of peptides 1 to 7 (Table S2); effect of temperature and pH on the activity and thermostability of myroilysin (Fig. S11); Lineweaver-Burk plots for the hydrolysis of casein by myroilysin at 50°C (Fig. S12).
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