Improving enantioselectivity of lipase from Candida rugosa by carrier-bound and carrier-free immobilization

2016 ◽  
Vol 130 ◽  
pp. 32-39 ◽  
Author(s):  
Susana Velasco-Lozano ◽  
Fernando López-Gallego ◽  
Javier Rocha-Martin ◽  
José Manuel Guisán ◽  
Ernesto Favela-Torres
Keyword(s):  
Candida Rugosa ◽  
Carrier Free ◽  
Lipase From Candida Rugosa

Carrier-Free Immobilization of Lipase from Candida rugosa with Polyethyleneimines by Carboxyl-Activated Cross-Linking

2014 ◽  
Vol 15 (5) ◽  
pp. 1896-1903 ◽  
Author(s):  
Susana Velasco-Lozano ◽  
Fernando López-Gallego ◽  
Rafael Vázquez-Duhalt ◽  
Juan C. Mateos-Díaz ◽  
José M. Guisán ◽  
...  
Keyword(s):  
Candida Rugosa ◽  
Cross Linking ◽  
Carrier Free ◽  
Lipase From Candida Rugosa

Immobilization of lipase from Candida rugosa on Sepabeads®: the effect of lipase oxidation by periodates

2011 ◽  
Vol 34 (7) ◽  
pp. 803-810 ◽  
Author(s):  
Nevena Ž. Prlainović ◽  
Zorica D. Knežević-Jugović ◽  
Dušan Ž. Mijin ◽  
Dejan I. Bezbradica
Keyword(s):  
Candida Rugosa ◽  
Lipase From Candida Rugosa

scholarly journals Improved Catalytic Performance of Carrier-Free Immobilized Lipase by Advanced Cross-Linked Enzyme Aggregates Technology

2021 ◽  
Author(s):  
Xia Jiaojiao ◽  
Yan Yan ◽  
Bin Zou ◽  
Adesanya Idowu Onyinye
Keyword(s):  
Low Cost ◽  
Immobilized Lipase ◽  
Candida Rugosa ◽  
Residual Activity ◽  
Candida Rugosa Lipase ◽  
Catalytic Performance ◽  
Functional Surface ◽  
Carrier Free ◽  
Effective Synthesis ◽  
Repeated Use

Abstract The cross-linked enzyme aggregates (CLEAs) are one of the technologies that quickly immobilize the enzyme without a carrier. This carrier-free immobilization method has the advantages of simple operation, high reusability and low cost. In this study, ionic liquid with amino group (1-aminopropyl-3-methylimidazole bromide，IL) was used as the novel functional surface molecule to modify industrialized lipase (Candida rugosa lipase, CRL). The enzymatic properties of the prepared CRL-FIL-CLEAs were investigated. The activity of CRL-FIL-CLEAs (5.51 U/mg protein) was 1.9 times higher than that of CRL-CLEAs without surface modification (2.86 U/mg protein). After incubation at 60℃ for 50 min, CRL-FIL-CLEAs still maintained 61% of its initial activity, while the value for CRL-CLEAs was only 22%. After repeated use for five times, compared with the 22% residual activity of CRL-CLEAs, the value of CRL-FIL-CLEAs was 51%. Further kinetic analysis indicated that the Km values for CRL-FIL-CLEAs and CRL-CLEAs were 4.80 mM and 8.06 mM, respectively, which was inferred that the affinity to substrate was increased after modification. Based on the above results, it was indicated that this method provided a new idea for the effective synthesis of immobilized enzyme.

scholarly journals Application of natural kaolin as support for the immobilization of lipase from Candida rugosa as biocatalsyt for effective esterification

2005 ◽  
Vol 29 (2) ◽  
pp. 111-116 ◽  
Author(s):  
Mohd Basyaruddin Abdul Rahman ◽  
Safarini Md Tajudin ◽  
Mohd Zobir Hussein ◽  
Raja Nor Zaliha Raja Abdul Rahman ◽  
Abu Bakar Salleh ◽  
...  
Keyword(s):  
Candida Rugosa ◽  
Lipase From Candida Rugosa
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