Faulds C B, Ralet M C, Williamson G, Hazlewood G P, Gilbert H J
Department of Food Molecular Biochemistry, Norwich Laboratory, UK.
Biochim Biophys Acta. 1995 Feb 23;1243(2):265-9. doi: 10.1016/0304-4165(94)00140-s.
Activity of an esterase from Pseudomonas fluorescens subsp. cellulosa (XYLD) on an insoluble feruloylated hemicellulose substrate (de-starched wheat bran) was dependent on the source of added endo-xylanase. The esterase exhibited high selectivity for the nature, position of linkage and size of the feruloylated oligosaccharides generated by hydrolysis of the hemicellulose. Increased affinity of XYLD with increasing size of the oligosaccharide substrate suggests that optimal activity is observed on substrates with at least 4 sugars.
荧光假单胞菌纤维素亚种（XYLD）的酯酶对不溶性阿魏酰化半纤维素底物（脱淀粉麦麸）的活性取决于添加的内切木聚糖酶的来源。该酯酶对由半纤维素水解产生的阿魏酰化寡糖的性质、连接位置和大小表现出高度选择性。随着寡糖底物大小增加，XYLD的亲和力增强，这表明在至少含有4个糖的底物上观察到最佳活性。
