3.9 Article

Utilization of Peach-palm waste for cost-effective amylase production by Trichoderma stromaticum: Stability and industrial potential

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TAYLOR & FRANCIS LTD
DOI: 10.1080/21501203.2023.2276728

Keywords

Agroindustrial waste; fungus; characterisation; optimisation; enzyme

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Amylases are important enzymes for biotechnological and industrial applications. In this study, amylase was successfully produced using peach palm waste as a low-cost substrate under solid state fermentation. The composition of the nitrogen source was optimized to further increase the amylase yield. The physicochemical characterization of the amylase revealed its optimum activity at pH 4.0 and temperature ranging from 50°C to 60°C. The enzyme showed stability in a wide range of pH and temperature conditions. This research demonstrates the potential of cost-effective amylase extraction for industrial applications, especially in food processes.
Amylases are among the most important enzymes for biotechnological and industrial applications. The present work aimed to analyse the use of agro-industrial waste as a low-cost substrate to the obtention of the amylase by the fungus Trichoderma stromaticum AM7 (CCMB617P) under solid state fermentation (SSF). The fungus was able to produce amylase using solely peach palm waste as a substrate (29.2 U/gds), however when a simplex centroid mixture design was applied to optimise the composition of the nitrogen source, peptone, and ammonium phosphate (7:3 w/w) in a total of 1% were added and an increase of the 45% (42.4 U/gds) was observed in relation to the activity initially obtained. The physicochemical characterisation of amylase revealed the optimum activity at pH 4.0 and temperature 50 degrees C to 60 degrees C. The amylase retained around 90% of its activity in a pH range from 4.0 to 7.0 and a temperature 40 degrees C to 70 degrees C, and 60% in a range from 80 degrees C to 100 degrees C, for up to 1 h. Amylase showed an increase in its activity with Al2+, Ag2+, and Co2+, however, the Cu(2+)negatively influenced the enzymatic activity. The enzyme was stable in the presence of SDS and beta-mercaptoethanol. The cost-effective enzyme extraction and stable amylase highlight its strong potential in industry applications, especially in food processes.

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