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العنوان
Biotechnological studies on some fungal industrial enzymes /
المؤلف
Tanash, Arafat Bedair El-Mewafey.
هيئة الاعداد
باحث / عرفات بدير الموافي طنش
مشرف / عبد الدايم ابو الفتوح شريف
مشرف / هدي محمد سليمان
مشرف / انوار توفيق منقريوس
الموضوع
Solid state fermentation (SSF). Industrial enzymes. lignocellulloses. Biodegradation. immobilization. half life time. successive.. mixed fermentation. agriculture wastes.
تاريخ النشر
2006 .
عدد الصفحات
212 p. :
اللغة
الإنجليزية
الدرجة
الدكتوراه
التخصص
علوم النبات
تاريخ الإجازة
1/1/2006
مكان الإجازة
جامعة المنصورة - كلية العلوم - Department of Botany
الفهرس
Only 14 pages are availabe for public view

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Abstract

Seventeen fungal species were isolated from six agriculture residues. However, Aspergillus niger, Aspergillus oryzae, Aspergillus flavus, Aspergillus terreus and Trichoderma viride were the most potents able to degrade different agriculture residues producing high yields of industrial enzymes such as; xylanase, cellulose, avicellase, CMCase, pectinase, arabinase, inulinase, amylase, dextrinase and phytase under solid state fermentation. Different fermentation culture conditions were studied on the effect of industrial enzymes production by Aspergillus niger and Trichoderma viride on barely bran. Aspergillus niger were the highest xylanase and pectinase producer, while, Trichoderma viride was the potent of CMCase and amylase production. The physiochemical and kinetic properties of industrial enzymes indicated that the studied enzymes were active at 40-50°C under pH levels ranged from 4.5-6.5. The activation energy of CMCase (4.58 Kcal mole-1) was lower compared with activation energy of xylanase (6.51 Kcal mole-1), amylase (10.54 Kcal mole-1) and pectinase (8.71 Kcal mole-1). Results also indicates that the enzymes were thermo-stable at 50 and 60°C This was clear by determination the half life values, deciminal reduction values and deactivation constants of each enzyme. The study was also investigated the immobilization technique of Aspergillus niger xylanase by different immobilization methods. Comparison between the physiochemical and kinetic properties of free and immobilized xylanase were indicated that immobilized xylanase was more stable at high temperature and wide range of pH levels. Furthermore, optimum temperature for its activity become 55°C instead of 45°C for free enzyme. However, optimum pH for immobilized xylanase was 4.5 instead of 5.5 of free enzyme. In addition, immobilization increased the values of half life time of enzyme (T1/2) and decrease the deactivation constant at different temperatures compared with free xylanase. In addition, the study was applied mixed and successive fermentation technique in the hope of finding more suitable fungal culture conditions that can degrade the hard lignocellulosic wastes more efficiently as well as production high titers of industrial enzymes.