Screening and optimization of the production of xylanase enzyme from streptomycetes
Mohamed S. Swelam ,Mohamed E. El awady, Mohamed I. El-khonezy, Mervat G. Hassan, Manal S. Selim and Sohier S. Abdel Salam
Xylan is recognized as the primary constituent of plant hemicelluloses and holds potential as a suitable initial material for synthesizing a range of artificial compounds and mixtures. Following cellulose, xylan ranks as the second most abundant polysaccharide found in the natural environment. The extraction of xylooligosaccharides from heteroxylans is achieved through both chemical and enzymatic approaches, with the latter method offering several advantages such as precision, substitution pattern and linkage type specificity, reaction manipulation, and elevated reaction rates. Xylanase is an innate enzyme present in organisms and fungi, falling under the category of pentosanases—an enzyme group used for breaking down plant cell wall matrices through xylan hydrolysis into xylose. Consequently, this inherent characteristic of the xylanase enzyme has bestowed it with commercial significance. Xylanases, classified as glucosidases (O-glycoside hydrolases, EC 3.2.1.x), facilitate the endo hydrolysis of 1,4-β-D-glycosidic bonds within xylan molecules. Among the most noteworthy xylanolytic microorganisms are Aspergilli, Trichoderma, streptomycetes, Bacilli, and others. In this investigation, twenty-one streptomycete isolates were obtained from various locations across Egypt and subjected to quantitative screening for xylanase production. The most potent isolate, Streptomyces (C5), was isolated from the Cairo region. Xylan and sodium nitrate were identified as effective carbon and nitrogen sources, respectively. The optimal pH for xylanase activity was determined to be 7, with an ideal temperature of 30°C, and an incubation period of seven days.