脂肪氧合酶是一种重要的食品酶。申请人前期研究发现，源于酿酒酵母Zuotin蛋白的自组装双亲短肽(SAP)与Pseudomonas aeruginosa脂肪氧合酶（LOX）的N-端融合，得到了热稳定性显著提升的融合酶（SAP-LOX）,这是国内外首次报道融合SAP提高酶热稳定性的研究。申请人拟以该SAP-LOX为研究对象，从三方面对其热稳定化机制进行系统研究：(1) 通过SAP-LOX晶体结构解析和分子动力学模拟，确定SAP引入的分子内相互作用与酶稳定化的定量关系；(2) 通过研究SAP-LOX寡聚体的形成及影响因素，探明SAP介导的分子间相互作用与酶稳定化的定量关系；(3) 基于强化SAP-LOX分子间和分子内相互作用，设计高热稳定化效能的SAP，并验证其通用性。研究得到的相关结论将深入揭示短肽融合促进酶稳定化的机制，同时为分子改造提供新的范例和思路。

Lipoxygenase is an important food enzyme. In our previous study, self-assembling amphipathic peptide (SAP) from zuotin protein sequence was fused to the N-terminus of Pseudomonas aeruginosa lipoxygenase (LOX), yielding a fusion enzyme (SAP-LOX) with an enhanced thermal stability. This is the first report regarding the enhancement of thermal stability of enzymes by fusing SAP. Taking the SAP-LOX as the object of study, we intend to carry out systematic researches on following three aspects: (1) Based on the crystal structure analysis and molecular dynamic simulation, we will the quantitative relationship between the thermal stability and intramolecular interaction added by SAP fusion; (2) By studying the formation of SAP-LOX oligomers and its influence factors, will examine the quantitative relationship between the thermal stability and interaction among SAP-LOX induced by SAP; (3) By strengthening the intermolecular and intramolecular interactions of SAP-LOX, we will design SAPs with high stabilization efficiency and the do the universality analysis. Conclusions making here will further enrich stabilization mechanism of enzyme fused with short peptide, and it will also provide new examples and ideas for molecular modification.