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Fig. 1 | Biotechnology for Biofuels

Fig. 1

From: Molecular and biochemical characterization of recombinant cel12B, cel8C, and peh28 overexpressed in Escherichia coli and their potential in biofuel production

Fig. 1

a Alignment of peh28-deduced residues with those of pectate lyase-6, cl19188, superfamily member PLN02793 as carried out using NCBI-CD-BLAST web-portal server. The Accession Numbers, gi 18412685, gi 224058683, gi 225442879, gi 255553121, and gi 297839921 represent the putative or hypothetical protein sources of Arabidopsis thaliana, Populus trichocarpa, Vitis vinifera, Vitis vinifera, Ricinus communis [58], while the tested peh28 sequence represented the line query. The black-shaded area represents the non-aligned sequences among all represented species compared to the others shown in the non-shaded region of the display. Peh28 showed high confidence similarity with the aligned protein sequences with overall domain specific threshold, bit score, of 116.13 and expectation-value, E value, 4.70e−29 from RPS-BLAST and PSSM mode of NCBI-CD-BLAST server, respectively. b Carbohydrate-binding domain (CBD) type II in cel112B protein sequence based on the alignment with those of other species using NCBI-CD-BLAST web-portal server. It shows two tryptophan residues that were found conserved among CBD-II of Pcc cel12B, query line, and the published sequences of endoglucanase D from Clostridium cellulovorans, 3NDZ_E, endoglucanase CelA from Streptomyces lividans, gi 121809, Cel12B from Cellulomonas fimi, gi 121813, and xylanohydrolase B from Cellvibrio japonicas, gi 294862476 according to Marchler-Bauer et al. [58]. The black-shaded area represents the non-aligned sequences among all represented species compared to the others shown in the non-shaded region of the display. Cel12B showed high confidence similarity with the aligned protein sequences with overall domain-specific threshold value, bit score, of 110.21 and E value, 1.40e-29 from the NCBI RPS-BLAST and PSSM mode servers, respectively

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