title: Preparation and Characterization of Immobilized Lipase from Pseudomonas Cepacia onto Magnetic Cellulose Nanocrystals.
abstract: Magnetic cellulose nanocrystals (MCNCs) were prepared and used as an enzyme support for immobilization of Pseudomonas cepacialipase (PCL). PCL was successfully immobilized onto MCNCs (PCL@MCNC) by a precipitation-cross-linking method. The resulting PCL@MCNC with a nanoscale size had high enzyme loading (82.2 mg enzyme/g) and activity recovery (95.9%). Compared with free PCL, PCL@MCNC exhibited significantly enhanced stability and solvent tolerance, due to the increase of enzyme structure rigidity. The observable optimum pH and temperature for PCL@MCNC were higher than those of free PCL. PCL@MCNC manifested relatively higher enzyme-substrate affinity and catalytic efficiency. Moreover, PCL@MCNC was capable of effectively catalyzing asymmetric hydrolysis of ketoprofenethyl ester with high yield of 43.4% and product e.e. of 83.5%. Besides, immobilization allowed PCL@MCNC reuse for at least 6 consecutive cycles retaining over 66% of its initial activity. PCL@MCNC was readily recycled by magnetic forces. Remarkably, the as-prepared nanobiocatalyst PCL@MCNC is promising for biocatalysis.
authors: State Key Laboratory of Pulp and Paper Engineering, South China University of Technology, Guangzhou 510640, China.|School of Chemistry and Chemical Engineering, South China University of Technology, Guangzhou 510640, China.
authors: Shi-Lin
authors: SL
authors: Cao
authors: State Key Laboratory of Pulp and Paper Engineering, South China University of Technology, Guangzhou 510640, China.
authors: Yu-Mei
authors: YM
authors: Huang
authors: School of Chemistry and Chemical Engineering, South China University of Technology, Guangzhou 510640, China.
authors: Xue-Hui
authors: XH
authors: Li
authors: State Key Laboratory of Pulp and Paper Engineering, South China University of Technology, Guangzhou 510640, China.|Lab of Applied Biocatalysis, School of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China.
authors: Pei
authors: P
authors: Xu
authors: Lab of Applied Biocatalysis, School of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China.
authors: Hong
authors: H
authors: Wu
authors: State Key Laboratory of Pulp and Paper Engineering, South China University of Technology, Guangzhou 510640, China.
authors: Ning
authors: N
authors: Li
authors: State Key Laboratory of Pulp and Paper Engineering, South China University of Technology, Guangzhou 510640, China.|Lab of Applied Biocatalysis, School of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China.
authors: Wen-Yong
authors: WY
authors: Lou
authors: School of Chemistry and Chemical Engineering, South China University of Technology, Guangzhou 510640, China.|Lab of Applied Biocatalysis, School of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China.
authors: Min-Hua
authors: MH
authors: Zong
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D055162:Biocatalysis; D002482:Cellulose / Q000737:chemistry; D004795:Enzyme Stability; D004800:Enzymes, Immobilized; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007660:Ketoprofen / Q000378:metabolism; D008049:Lipase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D058185:Magnetite Nanoparticles / Q000737:chemistry*; D011549:Pseudomonas / Q000201:enzymology*; D013696:Temperature
chemical_list: D001426:Bacterial Proteins; D004800:Enzymes, Immobilized; D058185:Magnetite Nanoparticles; D002482:Cellulose; D007660:Ketoprofen; D008049:Lipase