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首页> 外文期刊>Korean Journal of Microbiology and Biotechnology >Enzymatic Properties of Barley alpha-Amylase Chimeric Enzymes Produced by Staggered Extension Process
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Enzymatic Properties of Barley alpha-Amylase Chimeric Enzymes Produced by Staggered Extension Process

机译：交错扩展过程产生的大麦α-淀粉酶嵌合酶的酶学性质

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摘要

Barley malt produces two different alpha-amylase isozymes (AMY1 and AMY2), which share up to 80% of amino acid sequence identity with each other. However, their enzymatic properties differ remarkably. In this study, five chimeric enzymes between AMY1and 2 were constructed by staggered extension process (StEP) technique, and their enzymatic properties were characterized. According to the results, chimeric AMY-D2, D8, and E12 showed the mixed or intermediate types of calcium-dependent activity betweenAMYl and 2. Meanwhile, only AMY-EIO chimera could be significantly inhibited by barley a-amylase/subtilisin inhibitor (BASI) protein. Chimera AMY-C6 showed the same calcium-dependency as AMYl, while AMY-EIO was closely similar to AMY2. As a result, it can be proposed that some amino acid residues in the region II, III, and IV of barley a-amylases can play very important roles in the interaction with BASI, and those in III, V, VI, and VII may partly affect on the calcium-dependent activity.
机译：大麦麦芽产生两种不同的α-淀粉酶同功酶（AMY1和AMY2），它们彼此之间共享多达80％的氨基酸序列同一性。但是，它们的酶性质显着不同。在这项研究中，通过交错延伸过程（StEP）技术构建了AMY1和2之间的五个嵌合酶，并对其酶学性质进行了表征。根据结果​​，嵌合的AMY-D2，D8和E12显示AMY1和2之间存在钙依赖性活性的混合或中间类型。同时，只有AMY-EIO嵌合体可被大麦α-淀粉酶/枯草杆菌蛋白酶抑制剂（BASI）显着抑制。 ）蛋白。嵌合体AMY-C6显示出与AMY1相同的钙依赖性，而AMY-EIO与AMY2极为相似。结果，可以认为大麦α-淀粉酶的II，III和IV区的某些氨基酸残基在与BASI的相互作用中可以起非常重要的作用，而III，V，VI和VII中的那些可能部分影响钙依赖性活性。

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