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Erature and Shear Thinning Behaviour, Suggesting That Ovomucin Can Be Used As a Thickener and Stabilizer in Various Applications

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Erature and Shear Thinning Behaviour, Suggesting That Ovomucin Can Be Used As a Thickener and Stabilizer in Various Applications University of Alberta N-glycosylation and gelling properties of ovomucin from egg white by Marina Offengenden A thesis submitted to the Faculty of Graduate Studies and Research in partial fulfillment of the requirements for the degree of Master of Science in Food Science and Technology Department of Agricultural, Food and Nutritional Science ©Marina Offengenden Fall 2011 Edmonton, Alberta Permission is hereby granted to the University of Alberta Libraries to reproduce single copies of this thesis and to lend or sell such copies for private, scholarly or scientific research purposes only. Where the thesis is converted to, or otherwise made available in digital form, the University of Alberta will advise potential users of the thesis of these terms. The author reserves all other publication and other rights in association with the copyright in the thesis and, except as herein before provided, neither the thesis nor any substantial portion thereof may be printed or otherwise reproduced in any material form whatsoever without the author's prior written permission. Dedication To Ron, my shining sun on cloudy days Abstract Ovomucin is a bioactive egg white glycoprotein responsible for its gel-like properties and is believed to be involved in egg white thinning, a natural process that occurs during storage. Ovomucin is composed of two subunits: a carbohydrate-rich β-ovomucin and a carbohydrate-poor α-ovomucin. N- glycosylation of ovomucin was studied by nano LC ESI-MS, MS/MS and MALDI MS. Both proteins were N-glycosylated and site-occupancy of 18 potential N-glycosylation sites in α-ovomucin and two sites in β-ovomucin was determined. N-glycans of α-ovomucin were bisected complex-type glycans, while GlcNAc6Man3 was the most abundant glycan. In the second part, rheology and microstructure of aqueous ovomucin dispersions were studied. Ovomucin formed a fibrous network with weak gel properties in distilled water at room temperature and shear thinning behaviour, suggesting that ovomucin can be used as a thickener and stabilizer in various applications. In addition, influence of salt on ovomucin gel and its isoelectric point was determined. Acknowledgements I would like to thank my supervisor Dr. Jianping Wu for his advice, encouragement and guidance throughout my program that made the completion of this work possible. I highly appreciate the advice and suggestions I received from my supervisory committee members Dr. Mirko Betti and Dr. Michael Gaenzle. I would also like to thank Dr. Betti for allowing my access to his rheometer and Dr. Yang Liu for being my external examinator. Special thanks to Messele Fentabil for contributing his experience and knowledge in the area of mass spectrometry, MS results analysis and writing; to Dr. Jiapei Wang and Dr. Morshedur Rahman from whom I learned a lot. I am very grateful to all the wonderful people in the lab for their tremendous help and support during this time: Sahar Navidghasemizad, Kaustav Majumder, Jiandong Ren, Alexandra Acero-Lopez, April Milne, Dr. Shengwen Shen, Chamila Nimalaratne, Nandika Bandara, Dr. Aman Ullah, Dr. Chanchan Wang, Dr. Satyanarayana Bejjani, Dr. Sunjong You, Sen Li, Wenlin Yu, Yuchen Gu, Mejo Remanan, Ali Akbari, Justina Zhang, Xiuran Wang, Bushra Malik and Qi Yi Li. I would also like to thank Dr. Urmila Basu, Dr. Spencer Proctor and Kristina MacNaughton for access and help with Zetasizer, Dr. Jocelyn Ozga and Alena Jin, Dr. Randy Whittal and Jing Zheng from Mass Spectrometry Laboratory, Department of Chemistry; and Dr. Ming Chen for his help with electron microscopy. I would like to express my appreciation to the Poultry Research Centre (PRC), National Science and Engineering Research Council of Canada (NSERC) and Alberta Livestock Meat Agency Inc. (ALMA) for providing financial support for the research and the Graduate Student Association for the very helpful childcare subsidies. I am thankful to my parents Anatoly and Inna Tolchinsky, my grandmother Irina, brother Igor and my in-laws Regina and Dr. Yevsey Offengenden for their encouragement. Above all I would like to thank my husband Bernard Offengenden for his encouragement, support and understanding and my son Ron for always making me smile and lifting my spirits. Table of Contents CHAPTER 1. LITERATURE REVIEW ............................................................ 1 1.1 THE MUCINS: GENES AND STRUCTURE ........................................................... 1 1.1.1 The mucin family ................................................................................ 1 1.1.2 Secreted gel-forming mucins .............................................................. 2 1.1.3 Membrane-bound mucins ................................................................... 3 1.2 MUCIN GLYCOSYLATION ............................................................................... 4 1.2.1 Glycosylation types in mucins ............................................................ 4 1.2.2 N-glycosylation .................................................................................. 5 1.2.3 O-glycosylation .................................................................................. 7 1.3 THE BIOPHYSICAL PROPERTIES OF GEL-FORMING SECRETED MUCINS ............. 8 1.3.1 The structure and conformation of mucins in solution ...................... 8 1.3.2 The gelling properties of secreted gel-forming mucins ...................... 9 1.3.2.1 Influence of mucin concentration on gel formation ............ 10 1.3.2.2 Influence of polymeric structure and carbohydrate chains on gellation ........................................................................................... 10 1.3.2.3 pH-dependent gellation of porcine gastric mucin ................ 11 1.3.2.4 Influence of salts on mucin gels .......................................... 11 1.4 BIOLOGICAL ROLES AND APPLICATIONS ...................................................... 12 1.4.1 Mucins in interaction with bacteria ................................................. 12 1.4.2 Biomedical applications of mucins .................................................. 13 1.4.2.1 Mucoadhesion and drug delivery ......................................... 13 1.4.2.2 Mucin coatings on polymeric materials ............................... 14 1.4.2.3 Mucins as biomarkers for cancer ......................................... 15 1.5 OVOMUCIN – THE EGG MUCIN ...................................................................... 15 1.5.1 Ovomucin – the gelling agent of the egg white ................................ 15 1.5.2 The protein-rich subunit: α-ovomucin ............................................. 16 1.5.3 The carbohydrate-rich subunit: β-ovomucin ................................... 17 1.5.4 Ovomucin polymerization and rheology .......................................... 18 1.5.5 Egg white thinning – comparable process to the formation of 2 mucus layers? ............................................................................................ 19 1.5.6 Biological properties ........................................................................ 20 1.5.7 Applications ...................................................................................... 20 1.5.8 Objectives ......................................................................................... 21 1.6 LITERATURE CITED ..................................................................................... 23 CHAPTER 2. N-GLYCOSYLATION OF OVOMUCIN FROM HEN EGG WHITE ................................................................................................................. 35 2.1 INTRODUCTION ............................................................................................ 35 2.2 MATERIALS AND METHODS ......................................................................... 37 2.2.1 Materials .......................................................................................... 37 2.2.2 SDS-PAGE ....................................................................................... 38 2.2.3 In-gel PNGase F digestion ............................................................... 39 2.2.4 In-gel trypsin digestion .................................................................... 39 2.2.5 Nano LC-ESI MS and MS/MS Analysis ........................................... 40 2.2.6 Permethylation of N-glycans and MALDI-TOF MS and MS/MS ..... 40 2.2.7 Bioinformatic methods ..................................................................... 41 2.3 RESULTS ...................................................................................................... 41 2.3.1 Ovomucin subunits separation and identification by SDS-PAGE ... 41 2.3.2 Identification of N-glycosylation sites of α-ovomucin ...................... 42 2.3.3 Determination of site specific N-glycan structures by LC-MS/MS .. 43 2.3.4 Determination of N-Glycan profile of α-ovomucin by MALDI-TOF MS ............................................................................................................. 49 2.3.5 Motifs search in α-ovomucin sequence and alignment of its N- glycosylation sites with human MUC2 ...................................................... 51 2.4 DISCUSSION ................................................................................................. 51 2.5 LITERATURE CITED ..................................................................................... 56 CHAPTER 3. WEAK GEL PROPERTIES OF OVOMUCIN FROM HEN EGG WHITE ......................................................................................................
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