Purification and characterization of the extracellular lipase Lip2 from Yarrowia lipolytica

2007 ◽  
Vol 42 (3) ◽  
pp. 384-391 ◽  
Author(s):  
Mingrui Yu ◽  
Shaowei Qin ◽  
Tianwei Tan
Keyword(s):  
Yarrowia Lipolytica ◽  
Extracellular Lipase ◽  
Purification And Characterization

scholarly journals Gene cloning, expression, purification and characterization of a sn-1,3 extracellular lipase from Aspergillus niger GZUF36

2020 ◽  
Vol 57 (7) ◽  
pp. 2669-2680
Author(s):  
Shuqi Xing ◽  
Ruonan Zhu ◽  
Cuiqin Li ◽  
Laping He ◽  
Xuefeng Zeng ◽  
...  
Keyword(s):  
Aspergillus Niger ◽  
Gene Cloning ◽  
Extracellular Lipase ◽  
Purification And Characterization

Purification and Characterization of the Recombinant Form of Acyl CoA Oxidase 3 from the Yeast Yarrowia lipolytica

2000 ◽  
Vol 384 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Yi-Shan Luo ◽  
Hui-Jie Wang ◽  
K.V Gopalan ◽  
D.K Srivastava ◽  
Jean-Marc Nicaud ◽  
...  
Keyword(s):  
Yarrowia Lipolytica ◽  
Recombinant Form ◽  
Purification And Characterization ◽  
Acyl Coa Oxidase ◽  
Yeast Yarrowia Lipolytica

scholarly journals Characterization of an Extracellular Lipase Encoded by LIP2 in Yarrowia lipolytica

2000 ◽  
Vol 182 (10) ◽  
pp. 2802-2810 ◽  
Author(s):  
Georges Pignède ◽  
Huijie Wang ◽  
Franck Fudalej ◽  
Claude Gaillardin ◽  
Michel Seman ◽  
...  
Keyword(s):  
Amino Acid ◽  
Yarrowia Lipolytica ◽  
Lipase Activity ◽  
Alternative Pathway ◽  
Precursor Protein ◽  
Extracellular Lipase ◽  
Triacylglycerol Hydrolase ◽  
Amino Acid Precursor ◽  
Pro Region

ABSTRACT We isolated the LIP2 gene from the lipolytic yeastYarrowia lipolytica. It was found to encode a 334-amino-acid precursor protein. The secreted lipase is a 301-amino-acid glycosylated polypeptide which is a member of the triacylglycerol hydrolase family (EC 3.1.1.3 ). The Lip2p precursor protein is processed by the KEX2-like endoprotease encoded by XPR6. Deletion of the XPR6 gene resulted in the secretion of an active but less stable proenzyme. Thus, the pro region does not inhibit lipase secretion and activity. However, it does play an essential role in the production of a stable enzyme. Processing was found to be correct in LIP2 A (multipleLIP2 copy integrant)-overexpressing strains, which secreted 100 times more activity than the wild type, demonstrating thatXPR6 maturation was not limiting. No extracellular lipase activity was detected with the lip2 knockout (KO) strain, strongly suggesting that extracellular lipase activity results from expression of the LIP2 gene. Nevertheless, thelip2 KO strain is still able to grow on triglycerides, suggesting an alternative pathway for triglyceride utilization inY. lipolytica.

scholarly journals Production, Purification and Characterization of Extracellular Lipase from a Mutated Strain of Penicillium Citrinum KU613360

2021 ◽  
pp. 111-120
Author(s):  
Lakkakula Bhagya Lakshmi ◽  
M Raghu Ram
Keyword(s):  
Wild Strain ◽  
Strain Improvement ◽  
Lipase Production ◽  
Industrial Applications ◽  
Penicillium Citrinum ◽  
Extracellular Lipase ◽  
Purification And Characterization ◽  
Sds Page ◽  
Guntur District

In the present study lipase production, purification and characterization were carried out with a novel fungal strain of Penicillium citrinum KU613360 isolated from vegetable oil contaminated soil samples collected from oil mills located in and around Guntur District, Andhra Pradesh, India. The strain improvement was carried out by subjecting the strain to both UV and Ethidium Bromide treatments. The wild strain of P. citrinum KU613360 showed maximum lipase activity of 1.053±0.32IUmL-1 on optimized medium and while the mutated strain treated with combination of UV (300 sec) and Et Br (200 µgcm3), recorded the enzyme activity of 4.260±0.011IUmL-1, using the optimised medium at 6.5 pH and 40°C temperature. Thus, a 404% enhancement in the activity was achieved by using induced mutation on wild strain of P. citrinum KU613360. The molecular weight of the purified lipase from the mutated strain was found to be 35 kDa, when analysed on SDS PAGE. From our results it was concluded that the mutated strain has considerable capability and potentiality to be used in various industrial applications.

Purification and characterization of an extracellular lipase from a novel strain Penicillium sp. DS-39 (DSM 23773)

2011 ◽  
Vol 72 (3-4) ◽  
pp. 256-262 ◽  
Author(s):  
Dharmendra S. Dheeman ◽  
Sanjay Antony-Babu ◽  
Jesús M. Frías ◽  
Gary T.M. Henehan
Keyword(s):  
Extracellular Lipase ◽  
Purification And Characterization ◽  
Penicillium Sp
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