Purification and characterization of an endo-1,4-β-mannanase fromBacillus subtilisKU-1
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چکیده
منابع مشابه
Cell-wall-bound lytic activity in CMoreT/a /wsca; function and characterization of an endo-mannanase
A cell-wall-degrading activity was solubilized from young cells and from mother cell walls of CMo/W/a /w^ca by treatment with L i C l . The cytoplasmic enzyme hexokinase was not detectable in these extracts. The LiCl-solubilized activity increased in the cell cycle parallel to the release of autospores. The enzyme was purified on a chromatofocusing column followed by gel filtration. Sodium dode...
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Purification and Characterization of Leech Hyaluronic Acid-endo- P-glucuronidase*
In 1960, Linker, Meyer, and Hoffman (1) reported that a crude leech preparation hydrolyzes the glucuronide linkages of hyaluronic acid, unlike bacterial and testes hyaluronidases, which act on glucosaminide linkages. This paper deals with the first systematic attempt to purify the leech P-glucuronidase that specifically hydrolyzes hyaluronic acid. Purified preparations of the enzyme have indeed...
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An endo-exonuclease has been purified from cultured monkey (CV-1) cells. The enzyme which was purified to near homogeneity to be a 65 kDa monomeric protein. The single-strand DNase activity is endonucleolytic and nonprocessive, whereas the double-strand DNase activity is exonucleolytic and processive. The enzyme was also found to have RNase activity using poly-rA as substrate. The pH optimum fo...
متن کاملEndo-β-mannanase Activity in Tomato and Other Ripening Fruits
High amounts of endo-β-mannanase (EC 3.2.1.78) activity were extracted from tomato (Lycopersicon esculentum Mill.) fruits when a high-salt-containing buffer was used. Two pI forms of the fruit enzyme were identified, one being much more basic than the many seed isoforms. The number of isoforms increased if a protease inhibitor was not used during extraction. The enzyme was found in the ripe fru...
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ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 1998
ISSN: 0378-1097,1574-6968
DOI: 10.1111/j.1574-6968.1998.tb12795.x