| 扩展青霉（Penicilliumexpansum）PF868脂肪酶的纯化 … |
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| 引用本文： | 唐良华,王绍钊. 扩展青霉（Penicilliumexpansum）PF868脂肪酶的纯化 …[J]. 福建师范大学学报(自然科学版), 1999, 15(4): 80-84 |
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| 作者姓名： | 唐良华 王绍钊 |
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| 作者单位： | 福建师范大学生物工程学院!福州350007 |
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| 摘 要： | 扩展青霉（Ｐ．ｅｘｐａｎｓｕｍ）ＰＦ８６８所脂肪酶通过硫酸铵沉淀纤维素柱层析以及Ｓｅｐｈａｃｒｙｌ２００柱层析等步骤被纯化了７４倍。最终比活力为６９．７ｕ／ｍｇ。纯化后的脂肪酶经过ＳＤＳ－ＰＡＧＥ纯和微内径高效液相色谱纯。分子量经ＳＤＳ－ＰＡＧＥ确定为２８．４４ＫＤ。脂肪酶Ｎ－端氨基酸序列测定的结果是：ＡＴＡＤＡＡＡＡＦＰＤ－这与其他一些真菌产的脂肪酶的序列具有国闫的同源性。
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| 关 键 词： | 脂肪酶 纯化 氨基酸序列 扩展青霉 PF868 测定 |
| 修稿时间： | 1998-09-07 |
Purification and N-terminal Sequencing of the Lipase from Penicillium expansum PF868 |
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| Tang Lianghua Wang Shaozhao Shi Qiaoqin Wu Shonggang. Purification and N-terminal Sequencing of the Lipase from Penicillium expansum PF868[J]. Journal of Fujian Teachers University(Natural Science), 1999, 15(4): 80-84 |
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| Authors: | Tang Lianghua Wang Shaozhao Shi Qiaoqin Wu Shonggang |
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| Abstract: | The lipase from Penicillium expansum PF868 was purified 74 fold by ammoniumsulfate precipitation,DEAE Cellulose column chromatography and sephacryl 200 column chromatography to a final specific activity of 69.4 u/mg. The purified lipase showed homogeneous by SDS PAGE and Microbore HPLC. Its molecular weight was(28 44 kD)determined by SDS PAGE. The N terminal amino acid sequence of the enzyme was determined as follows:ATADAAAFPD.It shows a homology to the sequence of lipase from other fungi. |
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| Keywords: | lipase purification N terminal amino acid sequence Penicillium expansum |
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