Abstract

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.

Highlights

  • IntroductionThese enzymes actively take part in the breakdown of plant cell walls and other enzymes that hydrolyze polysaccharides and digest xylan during the germination of some seeds (e.g., in the malting of barley grain)

  • Particle size has a significant effect on xylanase production

  • This study reveals that the production of extracellular Xylanase under solid-state fermentation using lemon peels as one of the critical substrate material

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Summary

Introduction

These enzymes actively take part in the breakdown of plant cell walls and other enzymes that hydrolyze polysaccharides and digest xylan during the germination of some seeds (e.g., in the malting of barley grain). The heterogonous expression of the gene in A, encoding endo xylanase from Bacillus, in the yeast Saccharomyces cerevisiae has been described [1]. Endo-1, 4-β-xylanase Endo-1, 4-βxylanase (1,4-β-D-xylan hydrolase; EC 3.2.1.8) cleaves the glycosidic bonds in the xylan backbone, bringing about a reduction in the degree of polymerization of the substrate. Xylan is not attacked randomly, but the bonds selected for hydrolysis depend on the nature of the substrate molecule, i.e., on the chain length, the degree of branching, and the presence of substituent’s. Various literature reports; describe fermentative production of multienzyme using fruit peels such as those of Mango (Mangifera indica), Pomegranate (Punica granatum), Apple (Malus pumila), Mosambi (Citrus limetta), Banana (Musa acuminate), and Orange (Citrus reticulata) [2]

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