Effect of pH on ferulic acid production from sago bark by ceratocystis paradoxa for generating biovanillin

Vanillin is one ofthe most important and broadly utilised flavour chemicals in the food industry, as well as the major component of vanilla. In order to ensure a continuous supply of vanillin in low cost, a study focussing on biovanillin production by generating ferulic acid (FA) from agricultural-by-products was conducted with the aid of local isolate fungi, named, Ceratoeyetis paradoxa. Sago bark (SB), in chip form, was the major substrate to enhance the microbial bioconversion process as it could be acquired for a low cost. Furthermore, SB might contribute to environmental contamination as it was frequently released at nearby sago starch processing factory, if there are no systematic approach applied to reduce the bulky of SB. To ensure an efficient organisation of this study, three different pH values (pH 8.0, pH 9.0 and pH 10.0) had been examined, by standardising the optimal conditions such as temperature (28°C) and moisture constituent (70%) for the nourishing growth of Ceratoeyetis paradoxa in order to generate FAin high production from SB as the substrate via solid state fermentation (SSF). SSF was conducted under different pH values to determine the optimal pH condition and the enzyme responsible for microbial attack within the substrate. Production of FA and activity of ferulic acid esterase (F Ae) were the main findings for bioconversion process in this study. As a result, very low amount of FA produced from SB by Ceratoeystis paradoxa, as the highest FA production was in pH 8.0 on day 2, which was only 0.044 mg/g, with the enzyme activity of 0.089 U/g. This had proven that the chip form ofSB was not the relevant size for the microbial attack of Ceratoeystis paradoxa, relative to powder form of substrate, in generating FA for biovanillin production. The pH values below 8.0 had been proposed for future study of FA production by Cera toe yetis paradoxa as it might ensure the elevated yield with high enzyme activity