Heater Bradley S, Yang Zaofeng, Lee Marianne M, Chan Michael K
School of Life Sciences & Center of Novel Biomaterials, The Chinese University of Hong Kong, Hong Kong, SAR, China.
J Am Chem Soc. 2020 Jun 3;142(22):9879-9883. doi: 10.1021/jacs.9b13462. Epub 2020 May 19.
Cry3Aa is a protein that forms crystals naturally in the bacterium . Here we report that coexpression of Cry3Aa and a lipase without recombinant fusion results in the efficient passive entrapment of the lipase within the nanoporous channels of the resulting crystals. This Cry3Aa crystal-mediated entrapment provides multiple benefits to the lipase including a high enzyme loading, significantly improved thermostability, increased proteolytic resistance, and the ability to be utilized as a recyclable biodiesel catalyst. These characteristics, along with its greatly simplified method of isolation, highlight the potential of Cry3Aa crystal-mediated enzyme entrapment for use in biocatalysis and other biotechnological applications.
Cry3Aa是一种在细菌中自然形成晶体的蛋白质。在此我们报告，Cry3Aa与一种脂肪酶在无重组融合的情况下共表达，可使脂肪酶有效地被动包埋于所形成晶体的纳米多孔通道内。这种Cry3Aa晶体介导的包埋为脂肪酶带来了多种益处，包括高酶负载量、显著提高的热稳定性、增强的抗蛋白酶能力以及用作可循环生物柴油催化剂的能力。这些特性，连同其大大简化的分离方法，凸显了Cry3Aa晶体介导的酶包埋在生物催化及其他生物技术应用中的潜力。
