Optimum conditions for asparaginase extraction from Pisum sativum subspp. Jof. Zena Abdulla Khalaf, Nabeel Khalaf Al-Ani* and Hameed Majeed Jasim

نویسندگان: ثبت نشده
چکیده مقاله:

Asparaginase was extracted from plant parts of Pisum sativum subspp. Jof collected from a field crop. Asparaginase activity was detected in seeds, stems and leaves extracts. Enzyme activity was higher in seeds extracts (30.0 U/ml) compared with leaves extracts (26.4 U/ml) and stems extracts (16.1 U/ml), respectively. Optimum conditions for the activity of crude asparaginase extracted from plants seeds were studied. Results showed maximum activity of asparaginase was achieved when the enzyme was incubated with 200 mM of asparagines in a ratio of 1:3 (V/V) at 37 °C for 30 minutes in the presence of 0.05 M of potassium phosphate buffer solution at pH 8.Asparaginase activity was equal to 602.6 U/ml under optimum conditions.      

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Khalaf KHATATNEH Subject : Operators for complex modeling

Michel COTSAFTIS, Prof. LTME/ECE, Paris Referee Mohammad S. OBAIDAT, Prof. Monmouth University USA Referee Saleh OQEILI, Prof. Al-Balqa University Jordan, Referee Joël COLLOC, Prof. Le Havre University, Examiner Habib ABDULRAB, Prof. Rouen University, Guest Éric LAUGEROTTE A. Prof. Rouen University Guest Jean-Gabriel LUQUE, A. Prof. Gaspar Monge Institute, UMLV Guest Gérard DUCHAMP Prof. Galilé...

متن کامل

Asparaginase Isolated from Developing Seeds of Pisum sativum

Asparaginase (EC 3.5.1.1) was isolated from the developing seed of Pisum sativum. The enzyme is dependent upon the presence of K+ for activity, although Na+ and Rb+ may substitute to a lesser extent. Maximum activity was obtained at K+ concentrations above 20 millimolar. Potassium ions protected the enzyme against heat denaturation. The enzyme has a molecular weight of 68,300. Asparaginase acti...

متن کامل

DNA methylase from Pisum sativum.

DNA methylase activity was detected in nuclei from pea shoots. The enzyme can only be extracted by low-salt treatment if the nuclei are pretreated with micrococcal nuclease. Only a single enzyme was detected, and it was purified to a specific activity of 1620 units/mg of protein. It has an Mr of 160,000 on gel filtration and SDS/PAGE. Pea DNA methylase methylates cytosine in all four dinucleoti...

متن کامل

Optimum conditions for protein extraction from tuna processing by-products using isoelectric solubilization and precipitation processes

The by-product from tuna processing is a potential source of edible protein. Therefore, it is very important to extract protein from such raw materials for human food. In this study the optimum pH for protein extraction from tuna by-products was optimized by using isoelectric solubilization and precipitation processes. The Response Surface Methodology (RSM) and the single factor model were used...

متن کامل

Optimum conditions for protein extraction from tuna processing by-products using isoelectric solubilization and precipitation processes

The by-product from tuna processing is a potential source of edible protein. Therefore, it is very important to extract protein from such raw materials for human food. In this study the optimum pH for protein extraction from tuna by-products was optimized by using isoelectric solubilization and precipitation processes. The Response Surface Methodology (RSM) and the single factor model were used...

متن کامل

Anti -Hcv Lectin from Egyptian Pisum sativum

Lectins are carbohydrate binding proteins expressed in plants, animals and microorganisms and have been used to probe the surface properties of a wide range of prokaryotic and eukaryotic cells. The implication of some lectin molecules in several physiological processes has been claimed. The aim of this work is to purify the lectin from Egyptian pea (Pisum sativum) seeds and study its biochemica...

متن کامل

منابع من

با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ذخیره در منابع من قبلا به منابع من ذحیره شده

{@ msg_add @}


عنوان ژورنال

دوره 2  شماره 4

صفحات  517- 521

تاریخ انتشار 2012-08-01

با دنبال کردن یک ژورنال هنگامی که شماره جدید این ژورنال منتشر می شود به شما از طریق ایمیل اطلاع داده می شود.

میزبانی شده توسط پلتفرم ابری doprax.com

copyright © 2015-2023