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通过同源建模和分子对接对具有胰蛋白酶水解位点的新型鲜味八肽进行修饰

Modification of a Novel Umami Octapeptide with Trypsin Hydrolysis Sites via Homology Modeling and Molecular Docking.

作者信息

Cheng Kunya, Wang Shang, Wang Yian, Bao Yuxiang, Gao Pengxun, Lei Liming, Liang Huipeng, Zhang Sufang, Dong Liang

机构信息

School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, Liaoning, China.

National Engineering Research Center of Seafood, Dalian 116034, Liaoning, China.

出版信息

J Agric Food Chem. 2023 Apr 5;71(13):5326-5336. doi: 10.1021/acs.jafc.2c08646. Epub 2023 Mar 20.

DOI:10.1021/acs.jafc.2c08646
PMID:36939140
Abstract

Increasing the copy number of peptides is an effective method to genetically engineer recombinant expression and obtain umami peptides in large quantities. However, the umami taste value of multicopy number umami peptides is lower than the single ones, thus limiting the industrial application of recombinantly expressed umami peptides. With aims to solve this problem, modification of an umami beefy meaty peptide (BMP) with trypsin hydrolysis sites was carried out via homology modeling and molecular docking in this study. A total of 1286 modified peptide sequences were created and molecularly simulated for docking with the homology modeling-constructed umami receptor (T1R1/T1R3), and 837 peptides were found to be better docked than the BMP. Afterward, the MLSEDEGK peptide with the highest docking score was synthesized. And umami taste evaluation results demonstrated that this modified peptide was close to that of monosodium glutamate (MSG) and BMP, as confirmed by electronic tongue and sensory evaluation (umami value: 8.1 ± 0.2 for BMP; 8.2 ± 0.3 for MLSEDEGK peptide). Meanwhile, mock trypsin digestion of eight copies of MLSEDEGK peptide results showed that the introduced digestion sites were effective. Therefore, the novel modified BMP in this study has the potential for large-scale production by genetic engineering.

摘要

增加肽的拷贝数是进行重组表达基因工程并大量获得鲜味肽的有效方法。然而,多拷贝数鲜味肽的鲜味值低于单拷贝的,从而限制了重组表达鲜味肽的工业应用。为了解决这个问题,本研究通过同源建模和分子对接对具有胰蛋白酶水解位点的鲜味牛肉味肽(BMP)进行修饰。总共创建了1286个修饰肽序列,并对其进行分子模拟以与同源建模构建的鲜味受体(T1R1/T1R3)对接,发现837个肽的对接效果优于BMP。随后,合成了对接分数最高的MLSEDEGK肽。鲜味评价结果表明,这种修饰肽的鲜味接近味精(MSG)和BMP,电子舌和感官评价证实了这一点(鲜味值:BMP为8.1±0.2;MLSEDEGK肽为8.2±0.3)。同时,对八个拷贝的MLSEDEGK肽进行模拟胰蛋白酶消化的结果表明,引入的消化位点是有效的。因此,本研究中的新型修饰BMP具有通过基因工程进行大规模生产的潜力。

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