Physicochemical Modification of Kafirin Microparticles and Their Ability To Bind Bone Morphogenetic Protein-2 (BMP-2), for Application as a Biomaterial

被引:11
作者
Anyango, Joseph O. [1 ,2 ]
Duneas, Nicolaas [3 ]
Taylor, John R. N. [1 ,2 ]
Taylort, Janet [1 ,2 ]
机构
[1] Univ Pretoria, Inst Food Nutr & Well Being, ZA-0028 Hatfield, South Africa
[2] Univ Pretoria, Dept Food Sci, ZA-0028 Hatfield, South Africa
[3] Aids Biol, Pretoria, South Africa
关键词
kafirin; microparticle; cross-linking; binding; BMP-2; IN-VITRO; SECONDARY STRUCTURE; CONTROLLED-RELEASE; COLLAGEN SPONGES; WATER STABILITY; CROSS-LINKING; MAIZE ZEIN; DELIVERY; SORGHUM; DIGESTIBILITY;
D O I
10.1021/jf302533e
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
Vacuolated spherical kafirin microparticles with a mean diameter of 5 mu m can be formed from an acidic solution with water addition. Three-dimensional scaffolds for hard tissue repair require large structures with a high degree of interconnected porosity. Cross linking the formed kafirin microparticles using wet heat or glutaraldehyde treatment resulted in larger structures (approximately 20 mu m), which, while similar in size and external morphology, were apparently formed by further assisted assembly by two significantly different mechanisms. Heat treatment, which increased the vacuole size, involved kafirin polymerization by disulfide bonding with the microparticles being formed from round, coalesced nanostructures, as shown by atomic force microscopy (AFM). Kafirin polymerization, of glutaraldehyde-treated microparticles was not by disulfide bonding, and the nanostructures, as revealed by AFM, were spindle shaped. Both treatments enhanced BMP-2 binding to the microparticles, probably due to their increased size. Thus, these. Modified kafirin microparticles have potential as natural, nonanimal protein bioactive scaffolds.
引用
收藏
页码:8419 / 8426
页数:8
相关论文
共 55 条
[1]  
[Anonymous], 2005, Approved methods of the AACC
[2]   Improvement in Water Stability and Other Related Functional Properties of Thin Cast Kafirin Protein Films [J].
Anyango, Joseph O. ;
Taylor, Janet ;
Taylor, John R. N. .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2011, 59 (23) :12674-12682
[3]   Kafirin structure and functionality [J].
Belton, P. S. ;
Delgadillo, I. ;
Halford, N. G. ;
Shewry, P. R. .
JOURNAL OF CEREAL SCIENCE, 2006, 44 (03) :272-286
[4]  
Bessa PC, 2010, TISSUE ENG PART C-ME, V16, P937, DOI [10.1089/ten.tec.2009.0486, 10.1089/ten.TEC.2009.0486]
[5]   Alteration of kafirin and kafirin film structure by heating with microwave energy and tannin complexation [J].
Byaruhanga, Y. B. ;
Emmambux, M. N. ;
Belton, P. S. ;
Wellner, N. ;
Ng, K. G. ;
Taylor, J. R. N. .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2006, 54 (12) :4198-4207
[6]   Physicochemical properties and microstructure of soy protein hydrogels co-induced by Maillard type cross-linking and salts [J].
Caillard, R. ;
Remondetto, G. E. ;
Subirade, M. .
FOOD RESEARCH INTERNATIONAL, 2009, 42 (01) :98-106
[7]   Bone morphogenetic proteins [J].
Chen, D ;
Zhao, M ;
Mundy, GR .
GROWTH FACTORS, 2004, 22 (04) :233-241
[8]   The iso-electric points of various proteins [J].
Csonka, FA ;
Murphy, JC ;
Jones, DB .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1926, 48 (01) :763-768
[9]   Factors affecting sorghum protein digestibility [J].
Duodu, KG ;
Taylor, JRN ;
Belton, PS ;
Hamaker, BR .
JOURNAL OF CEREAL SCIENCE, 2003, 38 (02) :117-131
[10]   Characterisation of sorghum kafirins in relation to their cross-linking behaviour [J].
El Nour, INA ;
Peruffo, ADB ;
Curioni, A .
JOURNAL OF CEREAL SCIENCE, 1998, 28 (02) :197-207