NDLI: A serine protease inhibitor from Musca domestica larva exhibits inhibitory activity against elastase and chymotrypsin

Content Provider	Springer Nature Link
Author	Tang, Yan Wang, Ying Pei, Zhihuan Li, Wenting Zhang, Dandan Liu, Lei Kong, Lingcong Liu, Shuming Jiang, Xiuyun Ma, Hongxia
Copyright Year	2016
Abstract	Insect-derived serine protease inhibitors (serpins) exhibit multiple inhibitory activities, but so far, no functional roles for serpins of Musca domestica have been identified. Here, the functional features of M. domestica serine protease inhibitor (MDSPI16) were characterized.Hundred forty seven differentially expressed genes including the MDSPI16 gene were screened by constructing the subtractive cDNA library. The 1154-bp full-length MDSPI16 gene was cloned, and the recombinant MDSPI16 serpin protein was expressed as a 42.6 kDa protein in an Escherichia coli expression system. The recombinant MDSPI16 protein was purified using Ni–NTA affinity chromatography, and the inhibitory activity of MDSPI16 was assessed. MDSPI16 did not inhibit trypsin, papain, or proteinase K but strongly inhibited elastase (Ki = 2.8 nM) and chymotrypsin (Ki = 28 nM). The inhibitory activity of MDSPI16 remained stable over from 37 to 100 °C and from pH 2 to 12.The MDSPI16 exhibited inhibitory activity against elastase and chymotrypsin and the inhibitory activity remained stable.
Starting Page	1147
Ending Page	1153
Page Count	7
File Format	PDF
ISSN	01415492
Journal	Biotechnology Letters
Volume Number	38
Issue Number	7
e-ISSN	15736776
Language	English
Publisher	Springer Netherlands
Publisher Date	2016-04-04
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Chymotrypsin inhibitor Elastase inhibitor Gene cloning Musca domestica Protein expression Serine protease inhibitor Serpins Microbiology Biotechnology Applied Microbiology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Bioengineering Applied Microbiology and Biotechnology Biotechnology

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