4株细菌和8株真菌培养6d后，发现培养液中有机酸含量大幅度增加，pH大幅度地下降，磷的含量大幅度增加，真菌比细菌表现出更强的溶解磷矿粉的能力。不同的微生物分泌有机酸的数量和种类差别很大，真菌分泌的有机酸种类比细菌要多。但是，培养液中有机酸总量与解磷量之间并不存在显著的相关性。

从工业废水中分离的假单胞菌（Pseudomonas sp.）ND6菌株，能以萘为唯一碳源生长，使无机盐培养基（MM）中2g/L的萘在48h内降解98%。该菌株含有一个115kb的大质粒pND6。DNA杂交实验表明，pND6质粒含有与恶臭假单胞菌（P. putida）G7菌株的NAH7质粒同源的萘降解基因。图3表1参14

从3个不同地点采集的混合土壤中，分离到2株可利用2，4-二氯酚为唯一碳源和能源的假单胞菌（Pseudomonas sp.）DCP21和DCP22。在此基础上，研究探索了菌株DCP-1降解2，4-二氯酚的影响因素和降解过程以及其遗传特性。结果表明：菌株DCP21可降解2，4-二氯酚，并有氯离子、邻氯酚和醌积累；经检测该菌株中有一条迁移速率比pUC18小的质粒。

为了研究嗜甲基菌（Methylophilus）DM11菌株二氯甲烷脱卤素酶的不同氨基酸残基在底物结合、谷胱甘肽（GSH）亲和以及催化活力中的作用，对编码该酶的基因进行了定点诱变研究。将保守的103位色氨酸（W）分别用苯丙氨酸（F）、缬氨酸（V）或天冬酰胺（N）替换，109位精氨酸（R）用亮氨酸（L）替换，117位色氨酸用酪氨酸（Y）或苯丙氨酸替换，得到6种突变酶。其中3种突变酶具有较低的活力，另外3种突变酶没有活力。突变酶W117Y的性质与野生型酶明显不同。

Dichloromethane dehalogenase from Methylophilus sp. DM11 is a glutathione S-transferase homolog that is specifically active with dihalomethane substrates. This bacterial enzyme and rat liver glutathione S-transferases were purified to investigate their relative reactivity with CH2Cl2 and related substrates. Rat liver α class glutathione transferases were inactive and μ class enzymes showed low activity (7-23nmol/min/mg of protein) with CH2Cl2. θ class glutathione transferase 5-5 from rat liver and Methylophilus sp. Dichloromethane dehalogenase showed specific activities of≥1μmol/min/mg of protein. Apparen Kcat/Km were determined to be 3.3×104 and 6.0×104L M-1 S-1 for the two enzymes, respectively. Dideutereo-dichloromethane was processed to dideutereo-formaldehyde, consistent with a nucleophilic halide displacement mechanism. The possibility of a GSCH2X reaction intermediate (GS, glutathione; X, halide) was probed using CH2ClF to generate a more stable halomethylglutathione species (GSCH2F). The reaction of CH2ClF with dichloromethane dehalogenase produced a kinetically identifiable intermediate that decomposed to formaldehyde at a similar rate to synthetic HOCH2CH2SCH2F. 19F-NMR revealed the transient formation of an intermediate identified as GSCH2F by its chemical shift, its triplet resonance, and H-F coupling constant consistent with a fluoromethylthioether. Its decomposition was matched by a stoichiometric formation of fluoride. These studies indicated that the bacterial dichloromethane dehalogenase directs a nucleophilic attack of glutathione on CH2Cl2 to produce a halomethylthioether intermediate. This focuses attention on the mechanism used by θ class glutathione transferases to generate a halomethylthioether from relatively unreactive dihalomethanes.