[FTIR spectra analysis of the reactive activity of lignin when modified by laccase].
In company with the development of nonaqueous enzymology, the enzymatic modification of lignin has gained increasing interests, especially in the synthesis of high molecular material. In the present article, the enzymatic modification of spruce alkali lignin in cetyltrimethylammonium bromide (CTAB) reversed micelles (100 mmol x L(-1) 1, pH 6.0, W/O = 40), alcohol lignin in ethanol solution (50%), lignin sulphonate in sodium phosphate buffer (pH 5.8, 20 mmol x L(-1)) and steam-explosion wheat straw alkali lignin in alkaline solution (pH 10.0, 20 mmol x L(-1) NaOH) by mycelia sterilia YY-5 laccase was studied. Laccase was isolated from Mycelia Sterilia YY-5 (CGMCC-1462) which was an entophytic fungus of Rhus Chinensis Mill. FTIR spectrum was used to assay the structure of lignins and gel permeation chromatography (GPC) was used to determine the molecular weight and molecular weight polydispersity of lignins. Bands of lignin in FTIR spectra of all lignins changed obviously after treated with YY-5 laccase, which indicated that some bond breakage or rearrangement occurred to lignin. The shift of non-conjugated C=O and conjugated carbonyl groups (alpha-carbonyl groups) stretching vibration, the decrease of phenol hydroxyl stretching vibration and the increase of C--O--C stretching vibration of ester bond proved that phenolic hydroxyl, carbonyl group and side chain substituent all might participate in the laccase modification reactions of lignin. Meanwhile, the results of GPC indicated that the molecular of lignins all have certain increase and molecular polydispersity decreased. From the point of the molecular mass polydispersity, the modification effect of YY-5 laccase on steam-exploded wheat straw alkali lignin and spruce alkali lignin was more significantly than other two lignins. The molecular mass polydispersity for steam-exploded wheat straw alkali lignin and spruce alkali lignin was 1.211 and 1.375 respectively, which might contribute to the alkali-stable enzyme for YY-5 laccase. Correspondingly, alkali solution was chosen as the optimum medium for YY-5 laccase to modify lignins.
State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100190, China.
Wei-Hua
WH
Qiu
Hong-Zhang
HZ
Chen
D042845:Laccase / Q000378:metabolism*; D008031:Lignin / Q000737:chemistry*; D008970:Molecular Weight; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods*
D008031:Lignin; D042845:Laccase