从土样中分离筛选出产β-甘露聚糖酶的地衣芽孢杆菌，经紫外线诱变处理后（15W，30cm照射10s）获得高酶活力NK-27菌珠，在以魔芋粉、豆饼粉为碳、氮原添加无机盐的发酵培养基中，β-甘露聚糖酶活力达110.49μ/ml。初始pH值、装液量、培养温度和培养时间对产酶有一定影响。

由地衣芽孢杆菌（Bocillus Licheniformis）KN-27菌株产生的胞外β-甘露聚糖酶在40℃，pH值6.5～7.0，酶液终浓度10μ/g的条件下，酶解1%魔芋粉和瓜儿豆胶胶液1h后，所获得的酶解产物经薄板层板（展层剂∶正丁醇∶吡啶∶水=6∶4∶3，显色剂：笨胺-二苯胺-磷酸）检测表明为单糖和低聚糖。

由地衣芽孢杆菌NK-27获得的β-甘露聚糖酶在40℃、酶液终浓度1u/ml时，经12h水解魔芋粉、解豆胶、瓜儿豆胶和田菁胶所生成的酶解产物，经薄层层析检测表明为单糖和低聚糖。在PYG和GAM液体培养基中，添加不同量的四种植物胶酶解产物对青春双歧杆菌（Bifidobacterium adolescentis）具有明显的促生长作用，菌体增殖数从107提高到108个/ml。

A new engineering strain, Bacillus pumilus c172-14 (pBX 96), was obtained by introducing the pBX 96 plasmid, which carries the α-amylase amy gene, into the host strain of alkalophilic Bacillus pumilus c172 via transformation. The newly constructed strain was found to express the amy gene and could use starch instead of glucose or starch hydrolysate as carbon source for its fermentation of alkaline protease. The pBX 96 plasmid in the new host was found to be segregationally and structurally stable. The expression of amy gene did not affect the host strain's resistance to bacteriophages. Moreover, the level of alkaline protease was improved significantly compared with the parent strain. The constructed strain gave a maximum alkaline protease activity of 14, 014U/ml in shaking flask after 48h cultivation when growing in a medium containing 6% corn meal, 4% soybean flour, 0.4% Na2HPO4, 0.03% KH2PO4, 0.02% MgCl2, 0.3% CaCl2, 0.25% Na2CO3, 0.1% glucose, and 20μg/ml kanamycin (pH 7.0). The optimal pH value and temperature of the alkaline protease were 11.0 and 40℃, respectively. This enzyme was stable over a pH range of 8-11. Its residual activity remained at 100% when treated under a temperature of less than 45℃ for 30min. The corresponding residual activity reduced to 65% of its optimal value at 60℃ for 30min. The alkaline protease was a kind of serine protease, which was demonstrated by the complete inactivation by PMSF (1mM). This newly constructed strain will be useful in the alkaline protease industry.

以5, 5'-二硫硝基苯甲酸（DTNB）为柱前衍生试剂对酶促反应液进行衍生化，用C18色谱柱在室温下采用二元梯度洗脱，于330nm波长下检测，同时以2-巯基乙醇和二硫苏糖醇（DTT）为对照，对L-半胱氨酸的分离峰进行确认，并对酶促反应液中的L-半胱氨酸进行分离测定。L-半胱氨酸浓度为5～950μmol/L时，其浓度与峰面积呈显著的线性关系。高、中、低浓度水平的L-半胱氨酸加标回收率为99.7%～100.5%，相对标准偏差小于1.3%，检测限为0.8μmol/L。方法简便、快速、可靠。用于样品分析，结果令人满意。