Abstract
Saliva containing amylase was collected from an individual 5 min after a carbohydrate meal and filtered using a dialysis bag to remove starch particles. The filtered saliva was immobilized on calcium alginate beads. The effect of experimental parameters like pH, temperature and substrate concentration on the activity of the immobilized post-carbohydrate meal salivary α-amylase was determined. The immobilized salivary α-amylase had an optimum activity at temperature 40°C and pH 7.0. The activation energy (Ea) as obtained from the Arrhenius plot was 31.4 kJ/Mol. The kinetic parameters Km and Vmax of the immobilized α-amylase were found to be 1.6 mg/ml and 16.4 μmol/min, respectively; this was compared to that of free salivary α-amylase (Km = 0.0048 mg/ml) and α-amylases from fungi and bacteria sources. Immobilization tends to increase the Km of the immobilized enzyme, indicating a low affinity for substrate, however the enzymes Km was lower than that of some microbial α-amylases. The results obtained from the characterization of immobilized post-carbohydrate meal salivary α-amylase in this study show that immobilization had no significant effect on the enzyme and compared to kinetic parameters of microbial α-amylase, immobilized salivary α-amylase may not be of significant benefit as alternative source of α-amylase in the industrial bioprocesses. Key words: Enzyme activity, carbohydrate, immobilized enzyme, industrial bioprocess, kinetics, salivary α-amylase.
Highlights
Alpha amylases have been on increasing demand for various industries, due to their applications in the production of wide array of products, ranging from conversion of starch to sugar syrups, textile, paper, brewing, baking, distilling industries, preparation of digestive aids, production of cakes, and the production of cyclodextrins for the pharmaceutical industry (Sivaramakrishan et al, 2006; Gupta et al, 2003; Reddy et al, 2003)
The results obtained from the characterization of immobilized post-carbohydrate meal salivary α-amylase in this study show that immobilization had no significant effect on the enzyme and compared to kinetic parameters of microbial α-amylase, immobilized salivary α-amylase may not be of significant benefit as alternative source of α-amylase in the industrial bioprocesses
The result from the plot of immobilized post carbohydrate meal salivary α-amylase activity against temperatures values ranging from 25 to 70°C showed that temperature effect on the immobilized salivary α-amylase was optima at 40°C (Figure 1)
Summary
Alpha amylases have been on increasing demand for various industries, due to their applications in the production of wide array of products, ranging from conversion of starch to sugar syrups, textile, paper, brewing, baking, distilling industries, preparation of digestive aids, production of cakes, and the production of cyclodextrins for the pharmaceutical industry (Sivaramakrishan et al, 2006; Gupta et al, 2003; Reddy et al, 2003). These enzymes account for about 30% of the world’s enzyme production (Chi et al, 2009; Van der Maarel et al, 2002). The enzymatic hydrolysis is preferred to acid hydrolysis in starch processing industry due to a number of advantages such as specificity of the reaction, stability of the generated products, lower energy requirements and elimination of neutralization steps (Satyanarayana et al, 2005)
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