Kinetics of lactose conversion to galacto-oligosaccharides by β-galactosidase immobilized on PVDF membrane(BIOCHEMICAL ENGINEERING)
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概要
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Experimental studies were made for immobilization of enzymes on microporous polyvinylidene fluoride (PVDF) membrane in order to carry out enzymatic reaction of lactose into galacto-oligosaccharides using β-galactosidase. The present work, however, is the first part in the direction of enzymatic membrane reactor studies for carrying out reaction followed by membrane based separation to purify galacto-oligosaccharides out of reaction mixture. The middle of the three compartment cell, separated by two immobilized (enzyme) membranes, was utilized to feed lactose solution; whereas, adjacent compartments were filled with distilled water. The reacted mixture solution was analyzed for tri-, tetra- and penta-forms of GOS. The formation of product GOS strongly depended on varying amounts of initial lactose concentration (ILC). Total GOS formation increased from 7% to 28% for ILC from 50 to 200 g/L. However, tri-saccharide was the major (67%) in comparison to tetra (27%) and penta (6%) forms of GOS. Further, based on Michaelis-Menten kinetics, a six-step-eleven-parameter model was developed. The model incorporated enzyme inhibition and formation of glucose and galactose separately. Simulated results from developed model matched exceeding well with experimental results.
- 2013-06-00
著者
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Bhattacharya Prashant
Department of Chemical Engineering, Indian Institute of Technology Kanpur
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Palai Tapas
Department of Chemical Engineering, Indian Institute of Technology Kanpur
関連論文
- Kinetics and design relation for enzymatic conversion of lactose into galacto-oligosaccharides using commercial grade β-galactosidase(BREWING AND FOOD TECHNOLOGY)
- Kinetics of lactose conversion to galacto-oligosaccharides by β-galactosidase immobilized on PVDF membrane(BIOCHEMICAL ENGINEERING)
- Kinetics and design relation for enzymatic conversion of lactose into galacto-oligosaccharides using commercial grade β-galactosidase