Abstract：Hydrogen-bond states on cellobiohydrolase Ⅱ (CBHⅡ) of trichoderma viride were analysed by laser Raman spectroscopic method used to reveal molecular normal modes of vibration character. The results indicated that hydrogen-bond ability of carbonyl oxygen-atom of amideⅠ was raised in two types of aqueous solution samples(6.0 and 8.0 of pH value) compared to the solid sample. The variation trend of β structure modes was similar between amideⅡ and amideⅠ. As far as the ability of hydrogen-bond forming is concerned, tryptophan (Trp) and tyrosine (Typ) residues are strong hydrogen proton donor in pH 6.0 and solid sample，thus proving the results of previously spatial structure analysis. By analysis of free S—H character，the —S—S— construction in trichoderma viride mature paptide has been proved to be the same as that of trichoderma reesei.
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