Determination of β-galactosidase activity and kinetics in the crude extract of pleurotus ostreatus hyphae in the presence and absence of heavy metals

العناوين الأخرى

قياس النشاط و المعايير الحركية لأنزيم البيتا جلاكتوسيديز في مستخلص خيوط فطر المحار بوجود و عدم وجود المعادين الثقيلة

مقدم أطروحة جامعية

al-Shulul, Tariq Harun Rashid

مشرف أطروحة جامعية

Atruz, Umar

أعضاء اللجنة

al-Tarawinah, Khalid
al-Rawashidah, Ibrahim Muhammad
Mustafa, Ahmad

الجامعة

جامعة مؤتة

الكلية

كلية العلوم

القسم الأكاديمي

قسم الأحياء

دولة الجامعة

الأردن

الدرجة العلمية

ماجستير

تاريخ الدرجة العلمية

2016

الملخص الإنجليزي

The aim of this study was to measure the activity of β-galactosidase in Pleurotus ostreatus hyphae in the presence and absence of various heavy metals.

The enzyme β-galactosidase occurs widely in the nature and has been isolated from animal and plant sources as well as microorganism.β-galactosidase (EC 3.2.1.23), known as β-Gal, is a hydrolase enzyme which helps in the hydrolysis of lactose into monosaccharides. In this study, Extraction and characterization of β-galactosidase from Pleurotus ostreatus hyphae was achieved.

Characterization studies indicated that the enzyme extracted from Pleurotus ostreatus hyphae showed highest activity at pH 3, and the optimal temperature was found to be 40°C. The activity (Vmax ) of β-galactosidase enzyme using ONPG as substrate was found to be 0.571μmol/min, and Michaelis-Menten constant ( Km) was found to be 0.307 mM.

The results showed that the β-galactosidase activity in the crude extracts of Pleurotus ostreatus hyphae was changed in the presence of different heavy metals.

The results indicated that Hg2+ and Mo2+ have an uncompetitive inhibition on the β- galactosidase activity in the extract of Pleurotus ostreatus hyphae by decreasing both Km value from 0.307 mM to 0.285 mM and 0.253 mM, and Vmax from 0.571μmol/min to 0.189 and 0.377μmol/min, respectively.

While other heavy metals such as Al3+, Cu2+, Cr3+, Zn2+ and Ni2+ showed mixed inhibition on the β-galactosidase activity in the crude extract of Pleurotus ostreatus hyphae by decreasing Vmax from 0.571μmol/min to 0.476, 0.43, 0.363, 0.425 and 0.39 μmol/min, and by increasing Km from 0.307 mM to 1.162, 0.91,1.28, 0.66 and 0.892 mM, respectively.

However, Pb2+ showed non-competitive inhibition by decreasing Vmax from 0.571μmol/min to 0.408, and showed no change on Km value.

التخصصات الرئيسية

الرياضيات

عدد الصفحات

43

قائمة المحتويات

• APA
• MLA
• AMA

لغة النص

الإنجليزية

نوع البيانات

رسائل جامعية

رقم السجل

BIM-726128