Characterization of Thermo- and Detergent Stable Antigenic Glycosylated Cysteine Protease of Euphorbia nivulia Buch.-Ham. and Evaluation of Its Ecofriendly Applications
نویسندگان
چکیده
An antigenic glycosylated cysteine protease has been purified from the latex of Euphorbia nivulia Buch.-Ham. It exhibits remarkable protease activity in the presence of metal ions, oxidizing agents, organic solvents, and detergents. This enzyme showed potential role in leather processing industry due to its dehairing activity for animal hide without hydrolyzing fibrous proteins, producing, by this way, a better quality product. The enzyme can also be used for silver recovering from X-ray plates. In addition, the stability (temperature and surfactants) and hydrolysis of blood stain data also revealed its application in detergent industries. Agriculturally, this protease finds application in biocontrol process against the infectious management of root knot nematode, Meloidogyne incognita. Biologically, it shows noticeable wound healing, haemostatic and antibacterial activity.
منابع مشابه
Peptide Mass Fingerprinting and N-Terminal Amino Acid Sequencing of Glycosylated Cysteine Protease of Euphorbia nivulia Buch.-Ham.
A new cysteine protease named Nivulian-II has been purified from the latex of Euphorbia nivulia Buch.-Ham. The apparent molecular mass of Nivulian-II is 43670.846 Da (MALDI TOF/MS). Peptide mass fingerprint analysis revealed peptide matches to Maturase K (Q52ZV1_9MAGN) of Banksia quercifolia. The N-terminal sequence (DFPPNTCCCICC) showed partial homology with those of other cysteine proteinases...
متن کاملComparison of cysteine proteases of four laticiferous plants and characterization of Euphorbia nivulia Buch.-Ham. latex glycosylated cysteine peptidase
Investigations have been carried out on proteolytic activities of four laticiferous plants, viz. Calotropis procera (Ait.) R. Br. (Ruie), Carica papaya Linn. (Papaya), Euphorbia nivulia Buch.-Ham. (Sabar) and Ficus carica Linn. (Anjir) using Hammerstein grade casein and skimmed milk powder. Ratio of milk clotting to proteolytic activity was highest in the latex sample of C. papaya followed by F...
متن کاملMicrosciadin, a New Milk-Clotting Cysteine Protease from an Endemic Species, Euphorbia microsciadia
In the present work, a new branch of biotechnological advantage of the latex of an endemic perennial plant, Euphorbia microsciadia has been introduced. A novel cysteine protease, designated as microsciadin, was purified from the latex of Euphorbia microsciadia by a combination of sequential usage of SP-Sepharose Fast Flow column in two different pHs and a final gel filtration ...
متن کاملIn Vivo Evaluation of Genotoxic Effects of Euphorbia Nivulia Buch on Mice Bone Marrow Cells Using Chromosomal Aberration Test and Micro Nucleus Assay
Euphorbia nivulia is a tall deciduous tree belonging to the family Euphorbiaceae. It is mainly found in India and is reported to have tremendous therapeutic potential. Herbal medicine may cause damage to genetic material which may lead to an increased risk of cancer and other diseases. Hence, it becomes important to assess the genotoxicity assessment of herbal medicines. The present study was c...
متن کاملDigestive alkaline proteases from the Tunisian barbell (Barbus callensis): Characterization and application as a detergent additive, in chicken feather-degradation and as a dehairing agent
Alkaline crude enzymes from the viscera of the Tunisian barbel (Barbus callensis) were extracted and characterized. Proteolytic crude extract from barbel viscera was active and stable in alkaline solution. The optimum pH and temperature were 11.0 and 55 °C, respectively, using casein as a substrate. The crude alkaline protease was extremely stable in the pH range of 5.0-12.0. Zymography activit...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
دوره 2013 شماره
صفحات -
تاریخ انتشار 2013