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KMID : 1007519950040030189
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Food Science and Biotechnology
1995 Volume.4 No. 3 p.189 ~ p.193
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Estimation of the Hydrophobicity Changes in Coconut Proteins upon Heat Treatment
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Bae, Dongho
Lee, WonYoung/Choi, Yonghee
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Abstract
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The effects of heat treatments on the hydrophobicity of coconut proteins were studied using a fluorescent probe method. 8-anilino-1-naphthalene sulfonic acid (ANS) and all trans-retinol (RET) were used as hydrophobic probes to estimate the aromatic and aliphatic hydrophobicities (ARH and ALH) of coconut proteins. The number of ANS binding sites per unit protein increased from 0.45 for unheated samples to 1.28 for coconut proteins heated at 90℃ for 20 min, indicating 185.8% increase in ARH of coconut proteins. The number of RET binding sites increased from 0.25 to 0.99 with the same heat treatment, indicating 299.0% increase in ALH of coconut proteins. The increases in ARH and ALW with heat treatments showed similar trends with the increase in protein precipitation, verifying that the decreased solubility of coconut protein is caused by the increased hydrophobicity.
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