引用本文:	王淑军,邓祥元,李富超,秦松,陆兆新.耐高温酸性α-淀粉酶基因部分序列的克隆与分析[J].海洋科学,2007,31(12):69-75.

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耐高温酸性α-淀粉酶基因部分序列的克隆与分析
王淑军^1,2, 邓祥元³, 李富超³, 秦松³, 陆兆新¹
1.南京农业大学食品科技学院;2.淮海工学院,江苏省海洋生物技术重点建设实验室;3.中国科学院海洋研究所

摘要:

利用已报道的α-淀粉酶基因序列的保守区域设计引物,通过聚合酶链式反应(PCR)获得了高温球菌Thermococcus sp. HJ21的耐高温酸性α-淀粉酶基因的部分序列。通过对该序列的同源性比较分析发现,高温球菌Thermococcus sp. HJ21与热水高温球菌Thermococcus hydrothermalis和Thermococcus sp. OGL-20P的亲缘关系最近,序列相似度达到95%以上;利用Swiss Model预测该基因产物的3级结构,显示其具有典型的(β/α)₈桶状结构;通过分析密码子的使用情况得知,该α-淀粉酶存在着密码子的兼并性和使用的偏向性问题。

关键词: 高温球菌 α-淀粉酶基因克隆序列分析

DOI：

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基金项目:中国科学院知识创新工程重要方向项目(KZCX3-SW-223,KZCX2-YW-209);江苏省“六大人才高峰”第三批资助项目(06-A-017);江苏省教育厅自然科学基金项目(06KJB550004)

Cloning and sequence analysis of partial thermostable acid α-amylase gene

Abstract:

A fragment of α-amylase gene(1164bp) was cloned, sequenced and analyzed from a hyperthermophilic archae Thermococcus sp. HJ21 by PCR method, where the primers were designed via analysis of the known α-amylase on the website. The results of phylogenetic analysis showed that the similarities of α-amylase gene with homologous gene in Thermococcus hydrothermalis and Thermococcus sp. OGL-20P were over 95%. There were problems of degenerate and preference of codon usage in α-amylase through analysing the sequence of amimo acid. And the deduced protein three-tier structure of α-amylase with Swiss Model displayed that there was a typical(β/α)₈ structure on the protein three-tier structure.

Key words: Thermococcus α-amylase gene cloning sequence analysis