Fig. 2

Partial amino acid sequence alignment and SDS-PAGE results of pal1 and pal2 expressed in E. coli. a Partial amino acid sequence alignment of PAL1 and PAL2 of P. ostreatus CCMSSC00389 and other PALs. Positions with identical amino acid residues are indicated by circles below the sequence. (Pleurotus eryngii_AHH55203.1, Schizophyllum commune_XP_003030186.1, Coprinopsis cinerea_XP_001830572.2, Rhodosporidium toruloides_CAA31209.1, Arabidopsis thaliana_NP_181241.1). b SDS-PAGE analysis of recombinant PAL protein extracted from E. coli BL21 (DE3) cells. M, protein molecular weight standards; 1, crude lysate of pal1 from E. coli BL21 (DE3) grown at 16 °C for 12 h; 2, crude enzyme of pal1 from E. coli BL21 (DE3)/pSMART-V-PAL induced with IPTG (1 mM) at 16 °C for 12 h; 3, pal1 protein purified with a nickel column; 4, crude lysate of pal2 from E. coli BL21 (DE3) grown at 16 °C for 12 h; 5, crude enzyme of pal2 from E. coli BL21(DE3)/pSMART-V-PAL induced with IPTG (1 mM) at 16 °C for 12 h; and 6, pal2 protein purified with a nickel column. c Determination of PAL activity. Three independent biological replicates were performed for all experiments. The values are the means ± SE. Different letters indicate significant differences between the strains (P < 0.05, according to Tukey’s test)