Search In this Thesis
   Search In this Thesis  
العنوان
BIOLOGICAL CONTROL OF PINK BOLL WORM PECTINOPHRA GOSSYPIELLA BY DEGRADING ENZYMES PRODUCED from SOME MICROORGANISM
المؤلف
El-Sayed, Eman Mohammed Abd El-Azem
هيئة الاعداد
باحث / إيمان محمد عبد العظيم السيد
مشرف / أ.د/وسام عبد الغني حسانين
مشرف / أ.د/محمد أحمد ندا
مشرف / د/ فيفي محمد رضا
الموضوع
BIOLOGICAL CONTROL OF PINK BOLL WORM PECTINOPHRA GOSSYPIELLA MICROORGANISM
تاريخ النشر
2014
عدد الصفحات
192P.:
اللغة
الإنجليزية
الدرجة
ماجستير
التخصص
علوم النبات
تاريخ الإجازة
1/1/2014
مكان الإجازة
جامعة الزقازيق - كلية العلوم - النبات
الفهرس
Only 14 pages are availabe for public view

from 183

from 183

Abstract

The present work were carried out to study the biological activity of spores and supernatants of some actinomycetal isolates; Streptomyces chibaensis, Streptomyces vinaceusdrappus, Streptomyces albidofuscus and Streptomyces canarius; and bacterial isolates, Bacillus subtilis, Bacillus cereus and Pseudomonas aeruginosa. All isolates were isolated from soil and dead pink bollworm. The effect of these strains on percent of larval, pupal mortality, adult emergence and deformed adults were studied. Results revealed that mixed filtrates protease and lipase produced from Streptomyces vinaceusdrappus strain had highly significant effects on percent of larval mortality (50%) and (41.35%) in case of using bacterial filtrate of B. subtilis, comparing with control (13%). The mortality effects of these isolates were evaluated against 1st instar larvae of pink bollworm and their effects on other stages, pupae and adults. Identification of Streptomyces vinaceusdrappus was confirmed using 16s rRNA.
Streptomyces vinaceusdrappus was subjected to submerged fermentation under optimum conditions, at 30C and pH 7.0 in presence of 1% casein & 0.5% maltose while 0.5 % yeast & 1% sucrose for 6 and 5 days for lipase and protease, respectively under static conditions. Partial purification of protease and lipase were carried out by ammonium sulphate precipitation, dialysis, Sephadex G100 and finally Sephadex G50. The specific activities at final purification step of protease and lipase were 116.7 and 104.9 U mg-1 protein compared to 8.4 and 8.9 U mg-1 crude proteins, with yield 37 and 29 %, respectively. The both enzymes gave single homogenous band of 71 kDa by SDS- PAGE. Also, they had optimum pH 7.0 with stability from pH 7.0 – 11.0. The maximum enzyme activities obtained at 55 and 60°C with Tm values 86.5 and 83.9ەC for protease and lipase, respectively. The protease enzyme had high affinity and catalytic activity for casein followed by yeast-extract, albumen egg and gelatin while, the enzyme had low affinity to urea. Also the highest affinity was observed to olive oil followed by corn and coconut oils for lipase enzyme, while low affinity was to ricinus oil.The highest protease enzyme activity was exhibited in presence of