Cloning and expression of Aspergillus tamarii FS132 lipase gene in Pichia pastoris.
A lipase gene (atl) was cloned from Aspergillus tamarii FS132 for the first time. The gene was found to have an open reading frame of 1024 base pairs (bp), and the coding region of the gene contained two introns (51 bp and 52 bp). Multi-alignment analysis of the deduced amino acid sequence indicated high homology between the enzyme and mono-and diacylglycerol lipases from fungi Aspergillus. The recombinant lipase was expressed in Pichia pastoris GS115 cells. The recombinant lipase was found to have a molecular mass of 36.7 kDa, and it exhibited lipase activity of 20 U/mL in culture supernatant when tributyrin was used as the substrate.
Shi
Bihong
B
College of Life Sciences, Fujian Normal University, The University Town, Min-hou, Fuzhou 350108, China; E-Mails: zenglq_mail@163.com (L.Z.); songhl_mail@163.com (H.S.).
Zeng
Liqing
L
Song
Haolei
H
Shi
Qiaoqin
Q
Wu
Songgang
S
D000595:Amino Acid Sequence; D001230:Aspergillus / Q000145:classification / Q000201:enzymology / Q000235:genetics*; D003001:Cloning, Molecular; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D015870:Gene Expression; D008049:Lipase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D010802:Phylogeny; D010843:Pichia / Q000235:genetics* / Q000378:metabolism; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA
D005656:Fungal Proteins; D008049:Lipase