由链霉菌（Streptomyces sp.）S01菌株产生的几丁质酶（Chitinase）经硫酸铵盐析、DEAE纤维素柱层析、Sephadex G-100柱层析分离纯化后，得到SDS-PAGE均一样品。用SDS-PAGE测得纯化后的几丁质酶分子量为41Ku，用PAGEIEF测得等电点PI为5.4。酶反应的最适pH值为6.0，最适温度为50℃，在pH5.O～9.O、温度30～50℃时酶活性比较稳定。在相当于0.1mol/L NaCl的离子强度下酶活性最高。金属离子中的Mg2+、Ca2+、Mn2+对酶有较强的激活作用，而Fe3+、Hg2+则有强烈的抑制作用。S01菌几丁质酶对胶体几丁质的Km及Vmax分别为0.91mg·ml-1和262.13μmol·min-1·mg-1。

自70年代开始，国内曾筛选出短小芽孢杆菌（Bacillus pumilus）289、209两株产碱性蛋白酶的菌株。由于这两个菌株以葡萄糖为速效碳源，菌株产碱性蛋白酶的能力受培养基中总糖的制约，且两株菌易受短小芽孢杆菌烈性噬菌体PP1-PP10的感染，因而不利于作为碱性蛋白酶制剂生产用菌。作者已从制革厂毛泥池中分离得到一株碱性蛋白酶产生菌——短小芽孢杆菌c172，该菌株对PP1-PP10噬菌体不敏感，对地衣芽孢杆菌pL1噬菌体亦无交叉感染，是野生型的噬菌体抗性菌株[1]。c172菌无淀粉酶基因，仍以葡萄糖为碳源。为解除培养基中总糖含量对c172菌株产碱性蛋白酶的不利影响，采用原生质体转化手段将带有淀粉酶（Amy）、卡那霉素抗性（Kmr）和氯霉素抗性（Cmr）基因的pBX 96质粒导入c172菌株中，获得了c172（pBX 96）转化子。该转化子能够以玉米粉为碳源，经Amy基因编码的糖化型α-淀粉酶水解玉米粉后，水解物可为菌体生长和生产碱性蛋白酶持续提供碳源。本文报道c172（pBX 96）转化子碱性蛋白酶发酵条件的研究结果。

地衣芽孢杆菌（Bacillus licheniformis）NK-27菌株发酵产生的β-甘露聚糖酶（β-mannanase）经硫酸铵盐析沉淀，两次DEAE纤维素和Sephadex G-100离子交换柱层析以及制备PAGE等步骤，获得了凝胶电泳均一的样品。用SDS-凝胶电泳测得纯化后的β-甘露聚糖酶分子量为26kD，用凝胶聚焦电泳测得等电点PI为5.0。酶反应的最适pH为9.0，最适温度为60℃，稳定pH为6.0-9.0，稳定温度为40℃。金属离子中Mg2+、Ca2+、Fe2+、Fe2+、Ni2+对该酶有一定的激活作用；而Sn2+、Zn2+、Al3+、Ag+和Hg2+对该酶有强烈的抑制作用。NK-27菌株的β-甘露聚糖酶对魔芋葡萄甘露聚糖和角豆胶半乳甘露聚糖的Km值分别为7.14和5.56mg·ml-1；Vmax分别为200.53和157.45μmol·mg-1·min-1。

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。

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.