This study reports the synthesis of cellulose nanocrystal (CNC) from sugarcane bagasse and rice straw as the matrix for immobilized lipase enzyme. The CNC surface was modified using cetyltrimethylammonium bromide (CTAB) to improve the interaction of CNC with glutaraldehyde so that CNC can immobilize lipase effectively. The results showed that after surface modification of CNC using CTAB with concentrations of 2–10 mM, the crystallinity of CNC slightly decreased. The presence of immobilized lipase on the modified CNC was confirmed visibly by the appearance of dark spots using transmission electron microscopy (TEM). The bond formed between the enzyme and CNC was approved using Fourier transform infrared spectroscopy (FTIR). FTIR results show a new amine group peak in the immobilized lipase, which is not present in the modified CNC itself. The modified CNC, both from bagasse (SB-20 A1-1) and rice straw (RS-20 B1-1), was successfully applied to the immobilized lipase enzyme with a yield of 88%. The observed free enzyme activity was 3.69 µmol/min∙mL. The degree of hydrolysis of canola oil relative to free lipase (100%) from immobilized lipase at lipase SB-20 A1-1 and lipase RS-20 A1-1 was 23% and 30%, respectively. Therefore, this study successfully immobilized lipase and applied it to the hydrolysis of triglycerides.
The removal of 3-MCPD and GE from RBDPO was done through adsorption using activated carbon. The maximum 3-MCPD and GE removals result in 80% and 97%, respectively.
Over the past decade, the technology of enzyme immobilization has been developed because it is able to produce reusable immobilized enzymes to reduce production costs. This research aims to synthesize cellulose nanocrystals (CNC) from sugarcane bagasse. The CNC was then used as a matrix in immobilization of lipase to be applied in triglyceride lipolysis. Lipase was immobilized onto CNC through covalent bonding method at 25°C dan pH 7 with immobilization period variation of 0.5–4.5 hours. The immobilized lipase will be utilized to catalyze lipolysis reaction of triglyceride from palm oil, with lipolysis period 2–10 hours, reaction temperature of 25–60°C, and pH of 6.25–11.25. Lipase was successfully immobilized onto CNC so it can be utilized in lipolysis of palm oil with degree of hydrolysis about 10%. The optimum immobilization time and reaction time of lipolysis was 1.5 hours and 6–8 hours, respectively. Both free lipase and immobilized lipase had the optimum temperature at 40°C. In contrast to the optimum temperature, the optimum pH of the lipolysis reaction using free lipase is different from that of lipolysis using immobilized lipase. The optimum pH of lipolysis using free lipase is pH 7.25, while the optimum pH for reaction using immobilized lipase is shifted to pH 8.25.
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