To reveal the function of diacylglycerol acyltransferase (DGAT) on algae lipid production, DGAT from Chlorella variabilis NC64A was cloned and expressed by E.coli BL21 (DE3). The results showed that the DGAT gene was 894 bp and was coded 297aa. The apparent molecular weight of DGAT was 33 kDa and the pI was 9.48. Conserved domain analysis showed that it belonged to the Lysophospholipid acyltransferases (LPLATs) super family and the amino acids of H68, L71, F76, R94, I97 and GAA (144–146) could form special acyl acceptor binding pocket to bind acyl of ACP or CoA and served as the catalyst in the synthesis of TAG. Sequence analysis showed that DGAT shared a 32% and 24% homology with SsPDAT and AtPDAT respectively. Thin layer chromatography showed that DGAT had PDAT enzyme activity, which may promote the membrane lipid degradation and couple TAG synthesis under nitrogen starvation.

The present study was undertaken to investigate the enzyme characteristics of purified lignin peroxidase (LiP) from Pseudomonas sp. PKE117. The PKE117 LiP catalyzed veratryl alcohol oxidase activity at 25 ℃ showed that the optimum pH was 5.0, the optimum temperature at 30 ℃,　the K_m of the LiP was (0.277±0.000 8) mmol/L and the v_max was (0.049±0.001) mmol?mg^-1 protein?min^-1.The authors designed two special primers according to conservative sequences of lignin peroxidase and got a 199 bp DNA fragment (lip1) and a 563 bp DNA fragment (lip2). Sequence comparison demonstrated that lip1 and lip2 had low homology with known white rot fungi's lip genes. After translation, LiP1 had 100% homology with Pycnoporus sanguineus laccase, 80% homology with Mycobacterium bovis LiP. LiP2 had 100% homology with Arabidopsis thaliana LiP and 75% homology with Hordeum vulgare peroxidase 1.

The present study was undertaken to investigate the degradation ability and biological activity of purification lignin peroxidase (LiP) from Penicillium decumbens P6. P6 LiP had very good degradation ability on lignite, but its activity must depend on H₂O₂ activiation. After degradation, the contents of humic acid and fulvic acid increased distinctly, especially the content of fulvic acid. Results of elemental analysis indicated that the biodegraded products had higher H, O and N levels than the original lignite, although the carbon content was distinctly lower. The experimental molecular formula for lignite and its biodegraded products were C₁₀₀H_86.5O_36.5N_2.09 and C₁₀₀H_103.9O_48.6N_11.4 separately. The products of degradation could increase the germination rate and the speed of germination of pea. Furthermore, the authors designed two special primers according to N terminal amino acid sequence and got a 1956 bp cDNA fragment. Sequence comparison demonstrated that it had 45% homology with Piloderma croceum mnp2 gene and had conservative amino acids of catalase.