TITLE:
Isolation, Partial Purification and Characterization of Texas Live Oak (Quercus fusiformis) Lectin
AUTHORS:
Ruby A. Ynalvez, Carmen G. Cruz, Marcus A. Ynalvez
KEYWORDS:
Lectin, Quercus fusiformis, Protein Purification, HPLC, Blood Group Specificity, pH Stability
JOURNAL NAME:
Advances in Bioscience and Biotechnology,
Vol.6 No.7,
July
31,
2015
ABSTRACT: Lectins are carbohydrate-binding proteins with agglutination properties. There is a continuous interest in lectins due to their biological properties that can be exploited for medicinal and therapeutic purposes. The objective of this study was to isolate and characterize lectin activity in Texas Live Oak (Quercus fusiformis). More specifically, the study aimed to determine the lectin’s blood group specificity and pH stability, determine effects of seasonal variation, soil moisture and soil pH on lectin activity. The study also aimed to determine the presence of antifungal activity in Q. fusiformis extracts. Lectin activity was detected and compared via agglutination and protein assays. Protein partial purification was accomplished using diethylaminoethyl ion-exchange chromatography matrix. High Performance Liquid Chromatography (HPLC) was used to assess purity of the lectin. Results showed that Q. fusiformis extracts’ lectin activities are stable at a pH range of 5.2 - 9.2 but with a significant decrease in activity above pH 9.2. The lectin activity was significantly higher when assayed against sheep red blood cells as compared to other blood groups tested. Quercus fusiformis extract is devoid of antifungal activity against Aspergillus niger and Rhizopus stolonifer. The effects of seasonal variation, soil moisture and soil pH do not significantly correlate with lectin activity. Results from HPLC showed presence of three peaks indicating a partial purification of the Q. fusiformis lectin.