International journal of biological macromolecules, 130, 253-265 (2019-02-24)
Biocatalysts exerting activity against ester bonds have a broad range of applications in modern biotechnology. Some of the most industrially relevant enzymes of this type are lipolytic and their market is predicted to uphold leadership up till 2024. In this
Archives of biochemistry and biophysics, 667, 22-29 (2019-04-26)
A novel halophilic, alkalithermostable lipase LipR2 from Alkalispirillum sp. NM-ROO2 was cloned and expressed. LipR2 was covalently immobilized on Florisil® functionalized with glutaraldehyde. Protein binding efficiency of functionalized Florisil® was 94.7%. Immobilized LipR2 retained 97.5% of specific activity of the
The enzymatic properties of four lipases (A, B, C and D) from different strains of Aspergillus niger, were investigated, and a 3-factor mixture design and triangular surface analysis were performed to screen the optimal combi-lipase by observing synergistic effects. Lipases
Protein expression and purification, 138, 34-45 (2017-06-07)
Relatively poor heterologous protein yields have limited the commerical applications of Galactomyces geotrichum lipase I (GGl I) efficacy trials. To address this, we have redesigned the GGl I gene to preferentially match codon frequencies of Pichia pastoris (P. pastoris) while retaining
Journal of microbiology and biotechnology, 31(3), 483-491 (2021-02-25)
Two putative genes, lip29 and est29, encoding lipolytic enzymes from the thermophilic bacterium Geobacillus thermocatenulatus KCTC 3921 were cloned and overexpressed in Escherichia coli. The recombinant Lip29 and Est29 were purified 67.3-fold to homogeneity with specific activity of 2.27 U/mg
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