Zn2+ stapling of N and C-terminal maintains stability and substrate affinity in GH26 endo-mannanase.
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DOI: 10.1016/j.enzmictec.2019.109497
Abstract: Metal binding sites are present in one-third of proteins and are crucial for biological functions and structural maintenance. GH26 endo-mannanase (ManB-1601) from Bacillus sp. harbors a Zn2+ binding site which connects N (H1, H23) and… read more here.
Keywords: stability; endo mannanase; zn2 coordination; gh26 endo ... See more keywords
Biochemical analyses of a novel thermostable GH5 endo β-1,4-mannanase with minor β-1,4-glucosidic cleavage activity from Bacillus sp. KW1 and its synergism with a commercial α-galactosidase on galactomannan hydrolysis.
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DOI: 10.1016/j.ijbiomac.2020.10.235
Abstract: A novel GH5 endo-1,4-β-mannanase (BaMan5A) was identified from Bacillus sp. KW1, it shares the highest sequence identity (86%) with another characterized Bacillus endo-1,4-β-mannanase. The recombinant BaMan5A displayed maximum activity at pH 7.0 and 70 °C, it was… read more here.
Keywords: mannanase; gh5 endo; bacillus; endo mannanase ... See more keywords