Collected data suggest that raw aluminum hydroxide dried, milled and classified is a precursor for the new low temperature activated alumina transition phases, carrying distinctive characteristics and properties, due to products enrichment in amorphous phases. In our previous papers, there was studied the mechanisms of aluminum hydroxide phase transitions, during low temperature calcination, namely, at 260✬, 300✬, 400✬ and 600 ✬, under chosen particularly conditions, for promoting the nucleation of the amorphous phases. A wide range of literature on this subject is available, and recent reviews cover suitable information about preparation and characterization of different activated alumina products with specific properties and applications. The production of these arrays of useful material products is grounded on the multiple thermal decomposition pathways of Al(OH)3, which involve major crystallographic dislocations and many microstructure reconfigurations on variable lines of phase transitions, from the raw material up to large varieties of precursors and commercial grade products.
The properties of the enzyme showed that it has promising potential industrial applications for repeated utilization of the enzyme in both silver recovery and recycling of the X-ray film base.Īluminum hydroxide is a key product for the industrial production of alumiana and aluminium, ceramics insulator and refractories, desiccants, absorbents, flame retardants, filers for plastics and rubbers, catalysts, and various construction materials. Using a minimum concentration of bromelain (3 ml = 21.6 U) along with phosphate buffer (37 ml), it is possible completely to remove gelatin within 210 seconds. The enzyme was repeatedly used more than 50 times without significant loss of its activity. At optimum conditions (70☌ and pH 7.0), complete hydrolysis of the gelatin layer from X-ray film was observed at 30 and 34 seconds, respectively.
The optimum temperature and pH of the enzyme were recorded at 70☌ and pH 7.0, respectively. This implies that the enzyme is heat tolerant. The activity of a crude enzyme was 7.2 U/ml, and it was active in a broad range of pH (2.5–12) and temperature (25–85☌) without losing its activity. Extraction of bromelain was performed with a 1 : 2 ratio (w/v) of the extraction mix, pineapple fruit peel, in phosphate buffer (pH = 7.0). Therefore, the objective of this study was to characterize and investigate the potential application of bromelain enzyme extracted from pineapple juice processing waste peels in gelatin hydrolysis and removal of silver from X-ray films. However, bromelain from pineapple fruit peels is a less explored source for making valuable products. It has immense application in the pharmaceutical industry as well as in food, cosmetic, and leather industries. Bromelain is a proteolytic enzyme, which is predominately found in all parts of a pineapple plant (Ananas comosus).
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