Enzymatic in vitro glycosylation using peptide-N-glycosidase F

Ji Youn Lee; Tai Hyun Park

doi:10.1016/S0141-0229(02)00045-5

Enzymatic in vitro glycosylation using peptide-N-glycosidase F

Ji Youn Lee, Tai Hyun Park

Department of Nutritional Science & Food Management

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

Abstract

A high yield and cost effective process for the production of glycoproteins is attainable based on a low cost prokaryotic system with a high yield production of a nonglycosylated form, which is then glycosylated in vitro. Accordingly, the enzymatic deglycosylation of glycoproteins and enzymatic glycosylation of deglycosylated proteins were investigated using peptide-N-glycosidase F. Enzymatic in vitro glycosylation was found to occur with excess maltodextrin and ammonium salt in acetone at 50°C.

Original language	English
Pages (from-to)	716-720
Number of pages	5
Journal	Enzyme and Microbial Technology
Volume	30
Issue number	6
DOIs	https://doi.org/10.1016/S0141-0229(02)00045-5
State	Published - 27 May 2002

Bibliographical note

Funding Information:
The authors wish to acknowledge the financial support of LG Chemical Co. and the Nano Bio-Electronic & System Center.

Keywords

Deglycosylation
Glycosylation
Hydrazinolysis
Organic solvent
Peptide-N-glycosidase F

Access to Document

10.1016/S0141-0229(02)00045-5

Cite this

@article{993337f7971049858b96de84a8b9ee7c,

title = "Enzymatic in vitro glycosylation using peptide-N-glycosidase F",

abstract = "A high yield and cost effective process for the production of glycoproteins is attainable based on a low cost prokaryotic system with a high yield production of a nonglycosylated form, which is then glycosylated in vitro. Accordingly, the enzymatic deglycosylation of glycoproteins and enzymatic glycosylation of deglycosylated proteins were investigated using peptide-N-glycosidase F. Enzymatic in vitro glycosylation was found to occur with excess maltodextrin and ammonium salt in acetone at 50°C.",

keywords = "Deglycosylation, Glycosylation, Hydrazinolysis, Organic solvent, Peptide-N-glycosidase F",

author = "Lee, {Ji Youn} and Park, {Tai Hyun}",

note = "Funding Information: The authors wish to acknowledge the financial support of LG Chemical Co. and the Nano Bio-Electronic & System Center.",

year = "2002",

month = may,

day = "27",

doi = "10.1016/S0141-0229(02)00045-5",

language = "English",

volume = "30",

pages = "716--720",

journal = "Enzyme and Microbial Technology",

issn = "0141-0229",

publisher = "Elsevier Inc.",

number = "6",

}

TY - JOUR

T1 - Enzymatic in vitro glycosylation using peptide-N-glycosidase F

AU - Lee, Ji Youn

AU - Park, Tai Hyun

N1 - Funding Information: The authors wish to acknowledge the financial support of LG Chemical Co. and the Nano Bio-Electronic & System Center.

PY - 2002/5/27

Y1 - 2002/5/27

N2 - A high yield and cost effective process for the production of glycoproteins is attainable based on a low cost prokaryotic system with a high yield production of a nonglycosylated form, which is then glycosylated in vitro. Accordingly, the enzymatic deglycosylation of glycoproteins and enzymatic glycosylation of deglycosylated proteins were investigated using peptide-N-glycosidase F. Enzymatic in vitro glycosylation was found to occur with excess maltodextrin and ammonium salt in acetone at 50°C.

AB - A high yield and cost effective process for the production of glycoproteins is attainable based on a low cost prokaryotic system with a high yield production of a nonglycosylated form, which is then glycosylated in vitro. Accordingly, the enzymatic deglycosylation of glycoproteins and enzymatic glycosylation of deglycosylated proteins were investigated using peptide-N-glycosidase F. Enzymatic in vitro glycosylation was found to occur with excess maltodextrin and ammonium salt in acetone at 50°C.

KW - Deglycosylation

KW - Glycosylation

KW - Hydrazinolysis

KW - Organic solvent

KW - Peptide-N-glycosidase F

UR - http://www.scopus.com/inward/record.url?scp=0037182289&partnerID=8YFLogxK

U2 - 10.1016/S0141-0229(02)00045-5

DO - 10.1016/S0141-0229(02)00045-5

M3 - Article

AN - SCOPUS:0037182289

SN - 0141-0229

VL - 30

SP - 716

EP - 720

JO - Enzyme and Microbial Technology

JF - Enzyme and Microbial Technology

IS - 6

ER -

Enzymatic in vitro glycosylation using peptide-N-glycosidase F

Abstract

Bibliographical note

Keywords

Access to Document

Fingerprint

Cite this