{'fraction_non_alphanumeric': 0.043119266055045874, 'fraction_numerical': 0.03761467889908257, 'mean_word_length': 4.220095693779904, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Purification and Properties of Extracellular β β β β β-Glucosidase from the Antarctic Yeast Strain Cryptococcus Albidus AL 3

KOLEVA, L., I. PISHTIYSKI and K. PAVLOVA, 2006. Purification and properties of extracellular β-glucosidase from the Antarctic yeast strain Cryptococcus albidus AL 3 Bulg. J. Agric. Sci., 12: 713-720 Extracellular β-glucosidase from the Antarctic yeast strain Cryptococcus albidus AL 3 was isolated and purified by ultrafiltration, ion exchange chromatography and gel filtration. The purity of the enzyme preparations obtained was controlled by SDS-PAGE. The enzyme activity after gel filtration was 109 U/mg protein, the pH optimum was 5.0 and the temperature optimum was 45 0 C. This enzyme retained 18 - 20 % activity at 10 0 C. It was inhibited by glucose and activated by ethanol. Some metal ions sach as Cu +2 , Mg +2 and Mn +2 stimulated β-glucosidase activity, but it was inhibited by Hg +2 and Pb +2 . The enzyme was active against different β-glucosides. The kinetic parameters for p-Nitrophenil-β-Dglucopyranoside were K m 0.64 mMol and V max - 140 U/mg.