Religiosin B, a milk-clotting serine protease from Ficus religiosa
Religiosin B, a milk-clotting serine protease from Ficus religiosa
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DOI：
10.1016/j.foodchem.2011.09.122
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发表时间：
2012-04-15
期刊：
影响因子：
8.8
通讯作者：
Jagannadham, M. V.
中科院分区：
文献类型：
--
作者：
Kumari, Moni;Sharma, Anurag;Jagannadham, M. V.
从 Ficus religiosa 中纯化出一种新型凝乳丝氨酸蛋白酶，称为 religiosin B。该蛋白的分子量为63,000，pI值为pH 7.6。该酶的蛋白水解活性受到苯甲磺酰氟 (PMSF) 和糜抑素的强烈抑制。 Religiosin B 在 pH 8.0-8.5 和温度 55°C 时发挥最佳作用。该酶的摩尔吸收系数为 149,725 M-1 cm(-1)，每个酶分子有 23 个色氨酸、15 个酪氨酸和 7 个半胱氨酸残基。该酶对天然和合成底物表现出广泛的底物特异性。 Religiosin B 对变性剂和金属离子以及在广泛的 pH 值和温度范围内高度稳定。从头测序证实了该酶的新颖性。除了其高凝乳能力之外，它还可用于奶酪工业以及其他食品和生物技术工业。 (C) 2011 Elsevier Ltd. 保留所有权利。
A novel milk-clotting serine protease, named religiosin B, is purified from Ficus religiosa. The molecular mass of the protein is 63,000 with pI value of pH 7.6. The proteolytic activity of the enzyme is strongly inhibited by phenylmethanesulfonyl fluoride (PMSF) and chymostatin. Religiosin B acts optimally at pH 8.0-8.5 and temperature 55 degrees C. The molar absorption coefficient of the enzyme is 149,725 M-1 cm(-1) with 23 tryptophan, 15 tyrosine and 7cysteine residues per molecule of the enzyme. The enzyme shows broad substrate specificity with natural as well as synthetic substrates. Religiosin B is highly stable against denaturants and metal ions as well as over a wide range of pH and temperature. The de novo sequencing confirms the novelty of the enzyme. In addition to its high milk-clotting ability, it could be used in the cheese industry, as well as other food and biotechnological industries. (C) 2011 Elsevier Ltd. All rights reserved.