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Engineered yeast with PNGase F on cell surface for releasing of N-glycans from glycoproteins

Paper ID Volume ID Publish Year Pages File Format Full-Text
18238 42715 2007 7 PDF Available
Title
Engineered yeast with PNGase F on cell surface for releasing of N-glycans from glycoproteins
Abstract

Peptide-N-(N-acetyl-β-glucosaminyl) asparagine amidase F (PNGase F, EC 3.5.1.52) removes glycan moieties from glycoproteins under relatively mild conditions. This eznyme has been used as a powerful tool in analyzing the structural and biological functions of N-linked glycans of glycoproteins. The PNGase F gene from Flavobacterium meningosepticum was cloned into plasmid pYD1, which enabled regulated expression, secretion and detection. The expression of PNGase F gene at extracellular surface of Saccharomyces cerevisiae was confirmed by immunofluorescence microscopy. Fluorescence activated cell sorter analysis indicated that, after 36 h cultivation, 47.6% of the cell surface was anchored with target proteins. The surface engineered enzyme was confirmed to be active and reached its highest level after induced for 36 h. HPLC analysis showed that the specific activity of the surface-displayed PNGase F was about 12 U/g (cell dry weight).

Keywords
PNGase F; Yeast; Surface display; Biocatalyst
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Engineered yeast with PNGase F on cell surface for releasing of N-glycans from glycoproteins
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 40, Issue 6, 2 May 2007, Pages 1496–1502
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us