Fixed bed reactor performance of invertase immobilized on montmorillonite
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چکیده
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Modeling and Performance of Waste Tires as Media in Fixed Bed Sequence Batch Reactor
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متن کاملEnhanced pH and thermal stabilities of invertase immobilized on montmorillonite K-10
Invertase was adsorbed onto micro-porous acid-activated montmorillonite clay (K-10) by two procedures, namely adsorption and covalent binding. The immobilized enzymes were characterized by XRD, surface area measurements and Al NMR. XRD measurements revealed an expansion of clay layers due to immobilization which suggests that intercalation had taken place. Surface area measurements also support...
متن کاملImmobilized invertase.
Invertase is a commercially important enzyme used for the hydrolysis of sucrose. The hydrolysis of sucrose yields an equimolar mixture of glucose and fructose, known as invert syrup, is widely used in food and beverage industries. This enzyme is also used for the manufacture of artificial honey, plasticizing agents used in cosmetics, pharmaceutical and paper industries as well as enzyme electro...
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This study investigated the effect, on reactor performance and biomass retention inside the bed, of the material used to make the supports of anaerobic fixed-bed reactors. Three inert supports of similar shape but made of three different materials polyvinyl chloride, polypropylene, high-density polyethylene were manufactured and used. All three supports had the same specific surface area but di...
متن کاملComments on the behaviour of a fixed-bed reactor
Dear Sirs, In a recent series co-workers (see e.g. of papers by Morbidelli and Varma and Morbidelli and Varma 1986a; Morbidelli et al., 1986h Lee and Varma, 1987, 1988; Bauman and Varma 1990), the multiplicity behaviour of a fixed bed reactor is discussed. The basis for this analysis was given by Morbidelli and Varma (1986a) and Morbid& et al. (1986b), where the authors devote many columns to m...
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ژورنال
عنوان ژورنال: Catalysis Communications
سال: 2006
ISSN: 1566-7367
DOI: 10.1016/j.catcom.2005.12.029