| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 19451 | Food and Bioproducts Processing | 2011 | 5 Pages |
Abstract
Three AFPs (AFP-1, AFP-2, AFP-3) of Ligustrum lucidum Ait leaves were purified by using ice-affinity, chromatography separation on a DEAE-cellulose-32 column and a Sephadex G100 column. The ice-affinity proteins were about 1.2 mg/100 g leaves. Their molecular weight was 66.1, 26.3, and 20.2 kDa, respectively. Their thermal hysteresis activity was 0.379, 0.678, and 0.460 °C respectively. Asx was very abundant in these AFPs; its molar ratio was 22.2, 24.9, and 27.8%, respectively. AFP-2 was effective to protect peroxidase, β-glucosidase, and trehalose synthase from freeze–thawing process. Cryoprotection of AFP-2 is better than trehalose.
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Authors
Yujie Cai, Shang Liu, Xiangru Liao, Yanrui Ding, Jun Sun, Dabing Zhang,