【摘要】 根据抗冻蛋白与冰结合的特性,利用碎冰从女贞(Ligustrum lucidum)叶提取液中分离出抗冻蛋白。结果表明,通过碎冰吸附、凝胶过滤和离子交换层析可以获得4个组分的蛋白质,其中的1个经鉴定具有热滞活性。在蛋白质浓度为5mg.mL-1时,它的热滞活性(thermal hysteresis activity,THA)值为0.678°C,对其进行全波长扫描(200-1000nm)发现在975nm处有吸收峰;该蛋白亲水性氨基酸含量较高。更多还原

【Abstract】 According to the ice-binding characteristic, antifreeze proteins in the leaves of Ligustrum lucidum were isolated by adsorption to ice pieces at 0°C. Using Sephadex G-100 gel filtration and DEAE cellulose-52 anion exchange chromatography, we obtained 4 protein fractions, including a 36 kDa protein, identified as antifreeze proteins by differential scanning calorimetry. The THA value of the protein was approximately 0.678 °C when the protein concentration was 5 mg.mL-1. The maximal absorption peak was 975 nm after full-spectrum scanning from 200 to 1 000 nm. The content of hydrophilic amino acids was relatively higher than that of the other proteins.更多还原