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Register a new userCharacterization of β-galactosidase which was Isolated from New Born Goat Brain
توصيف إنزيم galactosidase – β المنقى و المستخلص من دماغ الماعز حديثة الولادة
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درست بعض خصائص إنزيم galactosidase-β المنقى و المستخلص من دمـاغ المـاعز حديثـة الولادة. و توصلت الدراسة إلى أن الإنزيم من نوع بروتين سكري، و تشكل مكونات الجزء الكربوهيـدراتي 1.22 % و ذلك بالاعتماد على طريقة فينول- حمض الكبريتيك. أما الدالة الحمضية (pH) المثلى لفعالية الإنزيم فقد كانت 5.5 و يفقد الإنزيم فعاليته كليا عند الدالـة الحمضية 5.8 ، و يظهر استقرارية عالية في المجال 4 - 6 من الدالة الحمضية. و أظهرت النتائج أن درجة الحرارة المثلى لفعالية الإنزيم °55C عند الدالة الحمـضية المثلـى. أمـا درجة الحرارة الملائمة لثبات الفعالية الإنزيمية فقد تراوحت بين °C 35 - 60 . و قد أظهر الإنزيم قدرة على حلمأة (Hydrolysis) (سكر اللاكتوز Lactose) بتركيز 5 % إذ تراوح مقدار الحلمهة بين 40 % بعد 60 دقيقة إلى 95 % بعد 270 دقيقة .
Some characteristics of β-galactosidase enzyme that was isolated from a new born goat brain were studied. This study concluded that the enzyme is glucoenzyme in which the carbohydrate part constitutes 22.1% in accordance with phenol –sulfate acid method. The optimum pH for the enzyme activity is 5.5. The enzyme lost its activity completely at pH8.5, and showed great stability at the range of pH 4-6. The results indicated that the optimum temperature for the enzyme activity is 55Co at the optimum pH. The stability temperature for the enzyme is 35-60Co. The analytical results of 5%lactose solution hydrolyzed by the enzyme have indicated that the hydrolysis rate is between 40% after 60 minutes, to 95% after 270 minutes.
References used
Abed, A. (2006). Isolation, Purification and Characterization of β-galactosidase From Local Chicken Liver. Ph. D. thesis. University of Baghdad. Iraq
Abed, A. (2010). Isolation and Purification of β-galactosidase From New Born Sheep Brain. Iraqi Journal for Sciences, No. 852, 65p
Abed Ali, A. (1989). Purification of Beta-galactosidase enzyme (Aspergillus's Niger) and studies of its kinetics. M. Sc. thesis. College of Sciences/ University of Baghdad
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β-galactosidase enzyme was isolated from the new born goat brain by nine
methods, It was found that the sodium acetate 0.2 Mole/Liter +0.2Mole/Liter
NaCl PH5 method have given the highest specific activity of crude enzyme in
comparison with the ot
her methods. Also, this enzyme was purified by using
four methods, the second one (cold acetone) was the butter. As a result the
purification fold was about 135.46 times and the yield about 77.14% by using
Sephacryl S200 (second step). This enzyme is 187.437 KDa as a molecular
weight.
40 samples were collected from milk from Homs to isolate the
bacteria and study their ability to produce the enzyme β-
galactosidase and diagnose isolates the most efficient in the
production of the enzyme, the results showed the presence of 25
sporeforming isolates producing the enzyme β-galactosidase , the
effectiveness of β-galactosidase was estimated using
spectrophotometer at a wavelength of 420 nm.
The enzyme was characterized by the following: Its molecular weight was 97
KD as estimated by gel filtration, iso electric point was at 6.2. The result
showed that it was a glycoprotein with a carbohydrate content of 13 % as
determined by phenol –
sulfuric acid method.
B-D-Galactosidase (B-D- galactoside galactohydrolase , E. C. 3.2.1.23) , is one of the most important enzymes used in food processing . It a specific example of a glycosidase enzyme. Many organisms naturally synthesize B- galactosidase , including mi
croorganisms , plants and animal cells . Among these possibilities , microbial sources are the best.
This study was carried out using white German goat race during 2000-2001
at the Research Center of Animal Production Division, Humboldt University,
Berlin, in order to examine the validity of the Lactocorder instrument, which
has been used for det
ermination of milking curve of cows, to determine the
milking curve of goat, and to study the timing changes of this curve.
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