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Xylanase is an enzyme that acts on xylan and degrades it into xylose. Xylanase may be produced by several different microbes such as bacteria and fungi. Xylanase has significant applications in food industries for improving dough handling and improving the quality of baked products in the extraction of starch, coffee, and plant oils. Xylanase, along with pectinase and cellulose, has enormous application in the clarification of fruit juices. In the present study, xylanase was produced by solid-state fermentation using lemon peel as substrates. Aspergillus Niger was induced to produce xylanase by frequent sub-culturing on a medium containing 2% xylan. OFAT was analyzed by using several fermentation parameters such as moisture content, particle size, incubation period, incubation temperature, peptone concentration, and pH of the extraction buffer. Under optimized conditions, the maximum xylanase activity was found for particle size of 1.7mm, moisture content of 80%, peptone concentration in nutrient solution at 0.3%, and extraction pH of 7.0. Hence, xylanase can be further subjected to down streaming processes and therefore for various applications.

The present research work emphasis on immobilization of lipase on PVA-alginate beads, which are used for biodiesel production via transesterification. The optimization of temperature, pH, and reusability of was performed on PVA-Alginate beads. The highest enzyme activity was found at a temperature of 40°C and pH 4.00. After six consecutive cycles of using the immobilized enzyme, the residual activity was 60% of the initial activity. The immobilized beads were stored at 4°C without buffer after 6 weeks, the immobilized enzyme retained 76.62% of initial activity.. The second-order mathematical model was developed using RSM. Transesterification process parameters were optimized by using ‘Full Factorial Design’ (FFD) with free lipase and immobilized lipase. The different factors considered for optimization were methanol/oil (M/O) ratio, reaction time, the weight of the catalyst with constant temperature and agitation speed. FFD was performed for free lipase, obtained the highest yield with optimum conditions; M/O ratio 9:1, reaction time 90 minutes, and weight of the catalyst was 0.3gm. Similarly, FFD was performed with immobilized lipase with the highest yield at 6:1 M/O ratio, 3 hours reaction time, the weight of the catalyst 3gm. FTIR was performed for the PVA-Alginate beads and lipase immobilized PVA-Alginate beads From FTIR spectra, the peaks shift from 1746 cm -1 to 1742 cm -1 signified the formation of biodiesel.