Effect of High Pressure Microfluidization on Functional and Conformational Properties of SPI

Abstract

Abstract: The effect of high pressure microfluidization (HPM) on functional properties and conformational properties of soy protein isolated(SPI) was investigated by measuring solubility, emulsification, hydrophobic properties, DSC thermogram and UV-CD spectrum. HPM could cause insoluble aggregates to dissociate, thus improving the solubility, emulsifying activity index(EAI) and hydrophobic properties of SPI. DSC analysis indicated Td remained basically unchanged, but ΔH tended to decline. UV-CD spectrum analysis showed that both the tertiary conformation and secondary structure of SPI were nearly unaffected by HPM treatment.

Key words: soy protein isolated (SPI), high pressure microfluidization, functional properties, conformation

CLC Number:

TS201.2

References

[1]苏丹，李树君等.超高压对大豆蛋白结构和功能性质影响研究进展[J].包装与食品机械,2009,27(5):111-115
[2]尹寿伟，唐传核，温其标，杨晓泉.微射流处理对芸豆分离蛋白构象和功能特性的影响[J].华南理工大学学报（自然科学版）,2009,37(10):112-116
[3]胡宝松，张绍英.超高压微射流破碎对大豆分离蛋白功能特性的影响[J].大豆通报,2007,4:30-34
[4] Sathe Dry bean protein functionality[J]. Critical Reviews in Biotechnology, 2002,22(2):175-223
[5]Iordache M.Jelen PHigh pressure micro-fluidization treatment of heat denatured whey protein for improved functionality[J]..Innovative Food Science and Emerging Technologies,2003,4(4):367-376
[6]Arrese E.L.,Sorgentini DA.,Wagner J.R.,et al.Electrophoretic,Solubility,and Functional Properties of Commercial Soy Protein Isolates[J]..Journal of Agricultural and Food Chenistry,1991,39:1029-1032
[7] E.Molina.,A.Papadopoulou.,D.A.Ledward.Emulsifying proerties of high pressure treated soy protein isolate and 7S and 11S globulin[J].Food Hyrocolloids 15(2001)263-269
[8]Li-Chan E.,Nakai S,Wood D.F.Hydrophobicity and solubility of meat protein and their relationship to emulsifying properties[J]..Journal of Food Science,1984,49:345-350
[9]M.C.Puppo..nullFperoni., N.Chapleau., M.de Lamballerie., M.C.Anon,. Effect of high-pressure treatment on emulsifying properties of soybean proteins[J].. Food Hydrocolloids,2005,19:289-
[10]Van der veen M., Norde W, Stuart M.C. Effects of Succinylation on the Structure and Thermostability of Lysozyme[J]..Journal of Agricultured and Food Chemistry,2005,53:5702-5707
[11]Jivotovskaya A.V., Vitalyi I, Vitalyi I. R., et al. Proteolysis of phaseolin in relation to its structure[J]..Journal of Agricultural and Food Chemistry,1996,44:3768-3772
[12]Romero J., Ryan DS. Susceptibility of the major storage protein of the bean,Phaseolus valgaris L., to in vitro enzymatic hydrolysis[J]..Journal of Agricultural and Food Chemistry,1978,26:784-788
[13]mtfield S.D., Murray ED. The influence of processing parameters on food protein functionality.I. Differential scanning calorimetry as an indicator of protein denaturation[J]..Cannadian Institute of Food Science and Technology Journal,1981,14:289-294
[14]Zirwer D.,Gast K, Welfle H., et al. Secondary structure of globulins from plant seeds:Are-evaluation from circular dichrosim measurements[J].. Internationl Journal of Biological Macromolecules,1985,7:105-108
[15]Kelly S.M., Jess TJ., Price N. C. How to study proteins by circular dichroism[J]., Biochimca et Biophysica Acta,2005,1751:119-139
[16] Pearce, K. N., & Kinsella, J. E. (1978). Emulsifying properties of proteins: Evaluation of a turbidimetric technique. Journal of Agricultural and Food Chemistry, 26, 716-723