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Register a new userIsolation and Purification of β-galactosidase From New Born Goat Brain
استخلاص و تنقية إنزيم galactosidase – β المستخلص من دماغ الماعز حديثة الولادة
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Damascus University ورقة بحثية
Publication date
2010
fields
Biology
and research's language is
العربية
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Shamra Editor
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عزل إنزيم galactosidase-β من دماغ الماعز حديثة الولادة باستخدام تسع طرائق، و قد وجد بأن طريقة 2.0 مول/ لتر من خلات الصوديوم + 2.0 مول/ لترمن كلوريد الصوديوم PH 5 هـي الطريقـة المثلى لاستخلاص الإنزيم و بأعلى فعالية نوعية له مقارنة ببقية الطرائق الأخرى التي استخدمت للغـرض نفسه. و رسب هذا الإنزيم باتباع أربع طرائق و قد تبين أن استخدام الأسيتون البارد هي الطريقة الفُضلى. و كان عدد مرات التنقية نحو 46.135 مرة و بلغت الحصيلة نحو 14.77 % عند استخدام الترشيح الهلامي 200-S Sephacryl) الخطوة الثانية). و بلغ الوزن الجزيئي للإنزيم 437.187 كيلو دالتون.
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 other 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.
References used
Abed, A. (2006). Isolation, Purification and Characterization of β-galactosidase From Local Chicken liver. Ph.D.thesis. University of Baghdad- Education College. Iraq
AL-Obaidy, H., 1975. Broad bean Lipoxygenase. M. Sc. Thesis, Food Sci. Dept. Agricultural college, Baghdad University
Al-Tamimi, S. (1996). The Enzymes Dissolving Proteins in Intact Grain, Abu Ghraib Variety, Infected with Sunna Insect and its Effect on Some Specific Characteristics. Ph.D. Thesis, College of Agriculture, Baghdad University
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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.
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.
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.
The study included the selection of the best methods to extract the enzyme
among nine methods. The protein content was concentrated and precipitated
by cold acetone among other five methods of concentration (partial
purification). The purification
stages were achieved by using ion exchange
column chromatography (DEAE – Sephadex A 50 column). Followed by gel
filtration chromatography using sephacryl S-300. The active parts were
lyophlizated (free drying) to obtain Lipoxygenase with 43.18% yield and 8.16
folds of purification and specific activity of 1162.9 unit / mg.
The purity of enzyme was confirmed by poly acryl amide gel
electrophoresis under non denaturing conditions, with the appearance a single
band .
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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