Modification of Glutamine and Lysine Residues in Holo and Apo -Lactalbumin with Microbial Transglutaminase

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• 作者：Willem F. Nieuwenhuizen ; Henk L. Dekker ; Leo J. de Koning ; Toos Grö ; neveld ; Chris G. de Koster ; and Govardus A. H. de Jong
• 刊名：Journal of Agricultural and Food Chemistry
• 出版年：2003
• 出版时间：November 19, 2003
• 年：2003
• 卷：51
• 期：24
• 页码：7132 - 7139
• 全文大小：99K
• 年卷期：v.51,no.24(November 19, 2003)
• ISSN：1520-5118

文摘

The molecular structures determine the physical properties of milk proteins and are important for thetexture of many dairy-based foods. Bovine ages/gifchars/alpha.gif" BORDER=0>-lactalbumin (ages/gifchars/alpha.gif" BORDER=0>-LA) is a globular 123 amino acid Ca²⁺binding milk protein. Modification with microbial Ca²⁺ independent transglutaminase (MTGase) wasused to modify lysines and glutamines in holo and apo ages/gifchars/alpha.gif" BORDER=0>-LA. At 30 ages/entities/deg.gif">C no lysines or glutamines aremodified in holo ages/gifchars/alpha.gif" BORDER=0>-LA, whereas in apo ages/gifchars/alpha.gif" BORDER=0>-LA lysines 13, 16, 108, and 114, and glutamines 39 and 43,are modified. At 50 ages/entities/deg.gif">C lysines 13, 16, 108, and 114, but no glutamines, are modified in holo ages/gifchars/alpha.gif" BORDER=0>-LA,whereas in apo ages/gifchars/alpha.gif" BORDER=0>-LA lysines 5, 13, 16, 108, and 114, and glutamines 39, 43, 54, 65, and 117, aremodified. The methods presented here offer the possibility to manipulate the availabilities of residuesin ages/gifchars/alpha.gif" BORDER=0>-LA to the MTGase reaction and enable the preparation of ages/gifchars/alpha.gif" BORDER=0>-LA species with different degreesof modification and hence with different physical properties.Keywords: Transglutaminase; ages/gifchars/alpha.gif" BORDER=0>-lactalbumin; calcium; mass spectrometry; protein structure