Difference between revisions of "Part:BBa K4724000"

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<p>CBM3 can be used to enhance the hydrophobicity of enzyme <sup>[1]</sup>, thereby enhancing the binding ability and affinity between the enzyme and the substrate, and ultimately achieving the purpose of improving enzyme activity. The CBM3 domain usually has flexibility and variability <sup>[2]</sup>, enabling it to adapt to the structural diversity of different substrates. It can adapt to different types of substrates through structural adjustment and closely bind to them. This adaptability and specificity help to enhance the binding ability and affinity between CBM3 and the substrate. This binding allows IsPETase to be closer to PET and bind to it, thereby increasing enzyme activity. In view of the fact that much literature has reported that CBM3 can promote the binding of enzymes to hydrophobic substrates, we chose CBM3 as our basic element to modify IsPETase to improve its binding ability and catalytic efficiency with the substrate PET.</p>
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<p>CBM3 can be used to enhance the hydrophobicity of enzyme <sup>[1]</sup>, thereby enhancing the binding ability and affinity between the enzyme and the substrate, and ultimately achieving the purpose of improving enzyme activity. The CBM3 domain usually has flexibility and variability <sup>[2]</sup>, enabling it to adapt to the structural diversity of different substrates. It can adapt to different types of substrates through structural adjustment and closely bind to them. This adaptability and specificity help to enhance the binding ability and affinity between CBM3 and the substrate. This binding allows IsPETase to be closer to PET and bind to it, thereby increasing enzyme activity. In view of the fact that much literature has reported that CBM3 can promote the binding of enzymes to hydrophobic substrates, we chose <i>CBM3</i> as our basic element to modify IsPETase to improve its binding ability and catalytic efficiency with the substrate PET.</p>

Revision as of 13:07, 9 October 2023


CBM3 can be used to enhance the hydrophobicity of enzyme [1], thereby enhancing the binding ability and affinity between the enzyme and the substrate, and ultimately achieving the purpose of improving enzyme activity. The CBM3 domain usually has flexibility and variability [2], enabling it to adapt to the structural diversity of different substrates. It can adapt to different types of substrates through structural adjustment and closely bind to them. This adaptability and specificity help to enhance the binding ability and affinity between CBM3 and the substrate. This binding allows IsPETase to be closer to PET and bind to it, thereby increasing enzyme activity. In view of the fact that much literature has reported that CBM3 can promote the binding of enzymes to hydrophobic substrates, we chose CBM3 as our basic element to modify IsPETase to improve its binding ability and catalytic efficiency with the substrate PET.