Peptidyl-Lys metalloendopeptidase (Lys-N) purified from dry fruit of Grifola frondosa demonstrates "mirror" digestion property with lysyl endopeptidase (Lys-C).

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2019
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Abstract
Lys-N, also known as lysine-specific metalloendopeptidase, functions as the "sister" enzyme of lysyl endopeptidase (Lys-C) in proteomic research. Its digestion specificity at the N-terminal lysine residue makes it a very useful tool in proteomics analysis, especially in mass spectrometry-based de novo sequencing of proteins. Here we invented a complete production process of highly purified Lys-N from dry fruit of Grifola frondosa (Maitake Mushroom). The purification process includes 1 step of microfiltration plus 1 step of UF/DF (ultra-filtrated used in tandem with diafiltrated method) recovery step and 4 steps of chromatography purification. The overall yield of the process was approximately 6.7 mg Lys-N protein/kg dry fruit of Grifola frondosa. The assay data demonstrated that the purified Lys-N exhibited high enzymatic activity and specificity. The novel production process provides the first time to extract of Lys-N from dry fruit of Grifola frondosa. The process is also stable, scalable, and provides an economic way of producing the enzyme in large quantities for mass spectrum-based proteomics and other biological studies.
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zhao2019peptidyllysrapid Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Mingzhi Zhao, Bingbing Hao, Honghao Li, Man Cai, Jingjing Xie, Hongyu Liu, Minjia Tan, Linhui Zhai, Qun Yu
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Journal Rapid communications in mass spectrometry : RCM
Year 2019
DOI
10.1002/rcm.8573
URL
Keywords
food allergy dendritic cell th2 cholera toxin

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