Proceedings Volume 2010 (format .pdf) - SimpBTH

XYLANASE PRODUCTION ON GLYCEROL - WHEAT BRANSUBSTRATEMIHAELA CLAUDIA MARINESCU 1 , GHEORGHE CAMPEANU 2 , CORINAIONESCU 1 , MISU MOSCOVICI 1 , RADU ALBULESCU 1 , MARIANA VLADU 11 National Institute for Chemical Pharmaceutical Research and Development – ICCF,Bucharest, Romania2 Center of Applied Biochemistry and Biotechnology - Biotehnol, Bucharest, RomaniaThe present study aimed the xylanase production by growing the microorganism Bacillusbrevis ICCF 500 using glycerol as a co-substrate with wheat bran.Biodiesel have drawn attention in the last decade as a renewable, biodegradable, and nontoxicfuel. Raw glycerol, byproduct from bio-diesel production process, is used as carbon substrate inseveral biotechnological applications.Using crude glycerol as a carbon source for fermentation is apromising alternative use for this waste material.The agricultural wastes, as wheat bran, are energy sources wich can be recovered byenzymatic strategies.Xylanases have made a remarkable impact in the world of biotechnology because of theirapplications in the pulp and paper, feed, food and fermentation industries. The most promisingapplication of xylanases is pre-bleaching of kraft pulp.The experiments were carried on , at laboratory scale, taking into account mediaoptimization in order to obtain the highest enzimatic activity.Key-words: xylanase, glycerol, wheat branINTRODUCTIONMicrobial enzymes are more advantageous than enzymes derived fromplants or animals because of their great variety of catalytic activities, possible highyields, stability, ease of genetic manipulation, regular supply due to absence ofseasonal fluctuations, rapid growth of microorganisms in inexpensive media, moreconvenient and safer protection methods.Xylanases (Endo-1,4-Beta-xylanase or XYN, EC 3.2.1.8) are glycosidaseswhich catalyze the endohydrolysis of 1,4-β-D-xylosidic linkages in the backboneof complex plant xylan polysaccharides [2].Plant cell walls are comprised of cellulose, hemicellulose and otherpolymers that are intertwined.This complex structure acts as a barrier todegradation by a single enzyme.Thus, a cocktail consisting of bi andmultifunctional xylanases and xylan debranching enzymes is most desiredcombination for the efcient utilization of these complex materials.First reported in 1955, they were originally termed pentosanases, and wererecognized by the International Union of Biochemistry and Molecular Biology(IUBMB) in 1961 when they were assigned the enzyme code EC 3.2.1.8. Theirofficial name is endo-1,4-b-xylanase, but commonly used synonymous terms224