Abstract
To gain further insight into the difference in substrate specificity between endoglucanase and cellobiohydrolase, the intrinsic fluorescence properties of cellobiohydrolase I (CBH I) and endoglucanase I (EG I) from Trichoderma pseudokiningii S-38 were investigated. The results for the spectral characteristics, ligand binding and fluorescence quenching suggest that the fluorescence of two enzymes comes from tryptophan residues, and that tryptophan residue(s) may be involved in the function of the two enzymes. The results also suggest that the binding tryptophan in EG I may be more exposed to solvent than that in CBH I. This interpretation is supported by the observations that the effects of pH upon the fluorescence of EG I are greater than that of CBH I; spectral shifts are different in EG I and CBH I under various conditions, and fluorescence lifetime changes caused by cellobiose binding are larger for EG I than for CBH I.
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Xu, Y.B., Qing, S.Y. & PeiJi, G. Intrinsic Fluorescence in Endoglucanase and Cellobiohydrolase from Trichoderma pseudokiningii S-38: Effects of pH, Quenching Agents, and Ligand Binding. J Protein Chem 16, 681–688 (1997). https://doi.org/10.1023/A:1026354403952
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DOI: https://doi.org/10.1023/A:1026354403952