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A thermostable lectin from the rhizomes of Kaempferia parviflora
Author(s) -
Konkumnerd Wichchulada,
Karnchanatat Aphichart,
Sangvanich Polkit
Publication year - 2010
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.4033
Subject(s) - lectin , rhizome , affinity chromatography , zingiberaceae , concanavalin a , chemistry , biochemistry , biology , traditional medicine , botany , enzyme , in vitro , medicine
BACKGROUND: Kaempferia parviflora , or black galingale (Kra‐Chai‐Dam), belongs to the Zingiberaceae family and is used as both a food ingredient and a medicinal plant. There are diverse reports on the biological activities of compounds extracted from the plant, such as antimalarial, antifungal and an effective sexual‐enhancing role, but not on the lectins. RESULTS: A lectin was isolated from the rhizomes of Kaempferia parviflora using affinity chromatography on Concanavalin A followed by gel filtration chromatography on Sephacryl S‐100. The molecular weight of the purified lectin was about 41.7 kDa. This lectin showed haemagglutinating activity against erythrocytes from several sources, with the highest level being against those from rabbits. Moreover, the lectin was thermostable, with significant haemagglutinating activity detectable up to 75 °C. The results of trypsin digestion and liquid chromatography/tandem mass spectrometry analysis suggested that this protein could be a member of the lectin/endochitnase1 family. CONCLUSION: A lectin that showed thermotolerant haemagglutinating activity against erythrocytes from several sources was successfully purified from K. paviflora rhizomes. Peptide sequence analysis indicated that this lectin is similar to lectin/endochitinase 1 ( Urtica dioica ) or Hevein‐like protein ( Hevea brasiliensis ). Copyright © 2010 Society of Chemical Industry