Bio-vaterite formation by glycoproteins from freshwater pearls

Antonino Natoli; Matthias Wiens; Heinz Christoph Schröder; Mauro Stifanic; Renato Batel; Analia L. Soldati; Dorrit E. Jacob; Werner E.G. Müller

doi:10.1016/j.micron.2010.01.002

Bio-vaterite formation by glycoproteins from freshwater pearls

Antonino Natoli, Matthias Wiens, Heinz Christoph Schröder, Mauro Stifanic, Renato Batel, Analia L. Soldati, Dorrit E. Jacob, Werner E.G. Müller^*

^*Corresponding author for this work

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

47 Citations (Scopus)

Abstract

A 48 kDa acidic and putative calcium-binding glycoprotein was isolated from pearls of the freshwater mussel Hyriopsis cumingii. This protein was compared with a related 46 kDa polypeptide, obtained from the nacreous shell of the same species. Separation by two-dimensional gel electrophoresis revealed that the difference in molecular weight is due to the higher extent of glycosylation of the 48 kDa protein existing in pearls. Evidence is presented that the sugar moieties of the protein contribute to crystal growth, starting with the nucleation step. In in vitro precipitation experiments, the 48 kDa glycoprotein of pearls directed the formation of round-shaped vaterite crystals while the 46 kDa glycoprotein of shells promoted formation of small irregular calcite particles. Furthermore, both proteins, 48 kDa/46 kDa, comprised carbonic anhydrase activity that has been implicated in CaCO₃ formation. Thus, a function of the isolated glycoproteins in biomineralization is proposed together with the mechanism by which they can stabilize different calcium carbonate polymorphs.

Original language	English
Pages (from-to)	359-366
Number of pages	8
Journal	Micron
Volume	41
Issue number	4
DOIs	https://doi.org/10.1016/j.micron.2010.01.002
Publication status	Published - Jun 2010
Externally published	Yes

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@article{cebfeb39143045a69d4be4fe124bf670,

title = "Bio-vaterite formation by glycoproteins from freshwater pearls",

abstract = "A 48 kDa acidic and putative calcium-binding glycoprotein was isolated from pearls of the freshwater mussel Hyriopsis cumingii. This protein was compared with a related 46 kDa polypeptide, obtained from the nacreous shell of the same species. Separation by two-dimensional gel electrophoresis revealed that the difference in molecular weight is due to the higher extent of glycosylation of the 48 kDa protein existing in pearls. Evidence is presented that the sugar moieties of the protein contribute to crystal growth, starting with the nucleation step. In in vitro precipitation experiments, the 48 kDa glycoprotein of pearls directed the formation of round-shaped vaterite crystals while the 46 kDa glycoprotein of shells promoted formation of small irregular calcite particles. Furthermore, both proteins, 48 kDa/46 kDa, comprised carbonic anhydrase activity that has been implicated in CaCO3 formation. Thus, a function of the isolated glycoproteins in biomineralization is proposed together with the mechanism by which they can stabilize different calcium carbonate polymorphs.",

keywords = "Biomineralization, Calcium carbonate precipitation, Carbonic anhydrase, Freshwater pearls, Vaterite",

author = "Antonino Natoli and Matthias Wiens and Schr{\"o}der, {Heinz Christoph} and Mauro Stifanic and Renato Batel and Soldati, {Analia L.} and Jacob, {Dorrit E.} and M{\"u}ller, {Werner E.G.}",

year = "2010",

month = jun,

doi = "10.1016/j.micron.2010.01.002",

language = "English",

volume = "41",

pages = "359--366",

journal = "Micron",

issn = "0968-4328",

publisher = "Elsevier Ltd.",

number = "4",

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TY - JOUR

T1 - Bio-vaterite formation by glycoproteins from freshwater pearls

AU - Natoli, Antonino

AU - Wiens, Matthias

AU - Schröder, Heinz Christoph

AU - Stifanic, Mauro

AU - Batel, Renato

AU - Soldati, Analia L.

AU - Jacob, Dorrit E.

AU - Müller, Werner E.G.

PY - 2010/6

Y1 - 2010/6

N2 - A 48 kDa acidic and putative calcium-binding glycoprotein was isolated from pearls of the freshwater mussel Hyriopsis cumingii. This protein was compared with a related 46 kDa polypeptide, obtained from the nacreous shell of the same species. Separation by two-dimensional gel electrophoresis revealed that the difference in molecular weight is due to the higher extent of glycosylation of the 48 kDa protein existing in pearls. Evidence is presented that the sugar moieties of the protein contribute to crystal growth, starting with the nucleation step. In in vitro precipitation experiments, the 48 kDa glycoprotein of pearls directed the formation of round-shaped vaterite crystals while the 46 kDa glycoprotein of shells promoted formation of small irregular calcite particles. Furthermore, both proteins, 48 kDa/46 kDa, comprised carbonic anhydrase activity that has been implicated in CaCO3 formation. Thus, a function of the isolated glycoproteins in biomineralization is proposed together with the mechanism by which they can stabilize different calcium carbonate polymorphs.

AB - A 48 kDa acidic and putative calcium-binding glycoprotein was isolated from pearls of the freshwater mussel Hyriopsis cumingii. This protein was compared with a related 46 kDa polypeptide, obtained from the nacreous shell of the same species. Separation by two-dimensional gel electrophoresis revealed that the difference in molecular weight is due to the higher extent of glycosylation of the 48 kDa protein existing in pearls. Evidence is presented that the sugar moieties of the protein contribute to crystal growth, starting with the nucleation step. In in vitro precipitation experiments, the 48 kDa glycoprotein of pearls directed the formation of round-shaped vaterite crystals while the 46 kDa glycoprotein of shells promoted formation of small irregular calcite particles. Furthermore, both proteins, 48 kDa/46 kDa, comprised carbonic anhydrase activity that has been implicated in CaCO3 formation. Thus, a function of the isolated glycoproteins in biomineralization is proposed together with the mechanism by which they can stabilize different calcium carbonate polymorphs.

KW - Biomineralization

KW - Calcium carbonate precipitation

KW - Carbonic anhydrase

KW - Freshwater pearls

KW - Vaterite

UR - http://www.scopus.com/inward/record.url?scp=77949487843&partnerID=8YFLogxK

U2 - 10.1016/j.micron.2010.01.002

DO - 10.1016/j.micron.2010.01.002

M3 - Article

SN - 0968-4328

VL - 41

SP - 359

EP - 366

JO - Micron

JF - Micron

IS - 4

ER -

Bio-vaterite formation by glycoproteins from freshwater pearls

Abstract

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