{'fraction_non_alphanumeric': 0.020590868397493287, 'fraction_numerical': 0.022381378692927483, 'mean_word_length': 5.576470588235294, '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}}
Amide hydrolyzing potential of amidase from halotolerant bacterium Brevibacterium sp. IIIMB2706

Abstract Till date, amidases from halophiles and halotolerant micro-organisms have not been much explored. In the present study, Brevibacterium sp. IIIMB2706 strain was isolated from salt fields of Gujarat, India, using propionitrile as a nitrogen source in the mineral base media and explored for its amidase activity. Amidase from Brevibacterium sp. IIIMB2706 exhibited substrate affinity towards isobutyramide, propionamide and butyramide. The optimum temperature and pH required for its maximum activity was 45 °C and 7.0, respectively. Effect of salt concentration on amidase activity was also studied and maximum activity was observed in presence of 50 g L−1 NaCl with significant activity up to 200 g L−1 NaCl which justifies its halotolerant nature. Various organic solvents compatibility profile showed that the enzyme was highly active in presence of 10% methyl alcohol. Henceforth, halotolerant enzymes may find application in industrial processes where substrate requires organic solvents for solubilization.