Characterization of glycosylated variants of {beta}-lactoglobulin expressed in Pichia pastoris期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

Characterization of glycosylated variants of {beta}-lactoglobulin expressed in Pichia pastoris

Authors:	Kalidas, Chitkala Joshi, Lokesh Batt, Carl

Affiliation:	¹ Field of Microbiology, Cornell University, Ithaca, NY 14853, USA ² Boyce Thompson Institute, Cornell University, Ithaca, NY 14853, USA ³ Department of Food Science, Cornell University, Ithaca, NY 14853, USA

Abstract:	Glycosylated variants of ß-lactoglobulin (BLG) wereproduced in the methylotrophic yeast Pichia pastoris to mimicthe glycosylation pattern of glycodelin, a homologue of BLGfound in humans. Glycodelin has three sites for glycosylation,corresponding to amino acids 6365 (S1), 8587 (S2)and 2830 (S3) of BLG. These three sites were engineeredinto BLG to produce the variants S2, S12 and S123, which carriedone, two and three glycosylation sites, respectively. The oligosaccharideson these BLG variants ranged from (mannose)₉(N-acetylglucosamine)₂(Man₉GN₂) to Man₁₅GN₂ and were of the

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