Abstract
This research assesses the bench-scale application of a non-conventional support, bone particles, for glucoamylase (GA) immobilization and its subsequent use in cassava starch hydrolysis. Upon determining the appropriate conditions to immobilize GA onto chicken bone particles, such as pH, ionic strength, particle size, and enzyme load, bench-scale immobilization of commercial GA without further purification was performed. Under the selected conditions, 270 GA units per gram of support were adsorbed. Optimal temperature and thermal stability of immobilized GA were only slightly different from those of the free enzyme, while optimal pH became more acidic by about one unit. The feasibility of the use of this immobilized biocatalyst for high glucose syrup production from liquefied cassava starch, at bench scale in batch process using a stirred-tank reactor, was demonstrated. Repeated use of the GA-bone derivative showed that similar conversions to those achieved with soluble enzyme (dextrose equivalent = 98) were reached until the third batch and over 90% until the 25th batch.
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Acknowledgments
This research was supported by the International Program in the Chemical Sciences (IPICS), Uppsala University, Sweden (project ECU-01). The support of LATSOBIO and LANFOOD-IPICS networks is specially acknowledged. The authors thank to Engrs. N. Espín, O. Proaño and P. Polit from Escuela Politécnica Nacional for their valuable contribution to the development of experimental work. Prof. Dr. Jan D. Miller, Chair Department of Metallurgy, College of Mines and Earth Science, University of Utah and Dr. Ximena Díaz are kindly acknowledged for the surface area analysis of the supports.
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Grant: International Program in the Chemical Sciences (IPICS), Uppsala University, Sweden (project ECU-01).
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Carpio, C., Escobar, F., Batista-Viera, F. et al. Bone-Bound Glucoamylase as a Biocatalyst in Bench-Scale Production of Glucose Syrups from Liquefied Cassava Starch. Food Bioprocess Technol 4, 566–577 (2011). https://doi.org/10.1007/s11947-008-0164-9
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DOI: https://doi.org/10.1007/s11947-008-0164-9