Assessment of the Morphological, Biochemical, and Kinetic Properties for <i>Candida rugosa</i> Lipase Immobilized on Hydrous Niobium Oxide to Be Used in the Biodiesel Synthesis

<table>Effect of reaction temperature on hydrolytic activities of lipase preparations. Enzymes were assayed with <i>p</i>-NPP as substrate at pH 7.0, (∘) free lipase, (●) niobium oxide-lipase. Starting activities (free lipase: 1868 units·mg<sup>−1</sup>; niobium oxide-lipase: 271 units·mg<sup>−1</sup>) were taken as 100%.</table>

Enzyme Research

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Figure 3

Figure 3: Assessment of the Morphological, Biochemical, and Kinetic Properties for <i>Candida rugosa</i> Lipase Immobilized on Hydrous Niobium Oxide to Be Used in the Biodiesel Synthesis 

Figure 3 | Assessment of the Morphological, Biochemical, and Kinetic Properties for Candida rugosa Lipase Immobilized on Hydrous Niobium Oxide to Be Used in the Biodiesel Synthesis 