NDLI: Expression and purification of the trypsin inhibitor from tartary buckwheat in Pichia pastoris and its novel toxic effect on Mamestra brassicae larvae

Content Provider	Springer Nature Link
Author	Ruan, Jingjun Yan, Jun Hou, Shengqi Chen, Hui Wu, Qi Han, Xueyi
Copyright Year	2014
Abstract	The gene of the trypsin inhibitor of tartary buckwheat (Fagopyrum tataricum) was successfully cloned, expressed in Pichia pastoris and tested for regulatory effects on insect growth. The three significant factors were optimized by single-factor experiments and central composite design in response surface methodology. Proteins were efficiently expressed at levels of 489.6–527.4 U/mg in shaken flasks. The trypsin inhibitor from tartary buckwheat (FtTI) was purified by affinity chromatography and centrifugal ultrafiltration. The purified FtTI efficiently inhibited trypsin protease activity by competitive inhibition with a Ki value 1.5 nM. The molecular mass of the purified protein was approximately 13.8 kDa. FtTI had a higher toxic killing effect on Mamestra brassicae larvae. The median lethal concentration for the larvae was 15 μg/mL.
Starting Page	209
Ending Page	216
Page Count	8
File Format	PDF
ISSN	03014851
Journal	Molecular Biology Reports
Volume Number	42
Issue Number	1
e-ISSN	15734978
Language	English
Publisher	Springer Netherlands
Publisher Date	2014-09-26
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Tartary buckwheat Trypsin inhibitor Cloning Expression Response surface methodology Mamestra brassicae Animal Biochemistry Animal Anatomy / Morphology / Histology
Content Type	Text
Resource Type	Article
Subject	Genetics Medicine Molecular Biology

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