热稳定细菌乳酸盐:催化特性及其在新兴污染物的生物转化中的应用
Varsha Panwar1, Stanzin Lzaod1, Tanmay Dutta1
1Enzyme Technology Laboratory, Department of Chemistry, Indian Institute of Technology Delhi, Hauz Khas, New Delhi 110016, India.
ACS omega
|October 2, 2023
概括
极度友好的细菌乳酸酶,如来自Brevibacillus agri的LacT,由于其稳定性和成本效益的生产,对工业应用有希望. 这项研究证实了LacT的存在.
科学领域:
- 生物技术和生物化学
- 酵素工程是什么? 酶工程是什么
- 环境科学 环境科学
背景情况:
- 菌乳酸主导着工业应用,但细菌乳酸具有极端稳定性和成本效益高的生产等优势.
- 极度友好的细菌乳糖因其对极端条件的弹性而受到大规模应用的关注.
- 此前已经报告了一种来自Brevibacillus agri的新型热稳定乳糖酶 (LacT).
研究的目的:
- 描述来自Brevibacillus agri.的耐热细菌乳糖酶 (LacT) 的特性.
- 调查LacT在生物修复性内分泌干扰物的潜力.
- 为了确认LacT在热应力下的序列相似性和结构完整性.
主要方法:
- 使用MALDI-TOF/MS-MS进行质指纹识别.
- 通过ICP-OES进行元素分析以确定铜含量.
- 谱分析 (CD,光) 和TGA以评估热稳定性.
- 酶性测试用于评估LacT对化合物的活性.
主要成果:
- LacT与CotA laccase具有很高的序列相似性,每分子约含有3.95个铜离子.
- 拉克显示出显著的热稳定性,在高温下保持结构完整性.
- 乳酸有效氧化了三桑和4,4'-二基双,在CuSO4和ABTS的存在下,氧化率提高.
- 仅在LacT和ABTS中观察到二醇转化,这表明了特定的基质相互作用.
结论:
- 细菌乳酶LacT是一种强大且耐热稳定的酶,具有工业应用的潜力.
- 对于特异性基内分泌干扰物,如三和4,4'-二基双,LacT对其生物修复有前途.
- 对LacT活动的进一步研究和与调解剂的优化可以扩大其生物修复能力.
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