• We are available for your help 24/7
  • Email: info@isindexing.com, submission@isindexing.com


Paper Details

Extraction and partial purification and sequencing of thaumatin-like protein (TLP) from barley and its screening for antimicrobial properties

Sindhuri Madineni

Journal Title:Journal of Chemical, Biological and physical sciences
Abstract


Thaumatin like proteins (TLPs) are the products of a large, highly complex gene family involved in host defense mechanism and belongs to pathogenesis related proteins of group 5. TLPs show homology with thaumatin, a sweet tasting protein from fruits of Thaumatococcus danielli. TLPs have glucan binding and glucanase activities. The current study reported the extraction, purification and sequencing of TLPs from Hordeum vulgare grains. A protein with an apparent molecular mass of 22 KD, which was one of the most abundant proteins in extracts of barley grains was purified by ion exchange chromatography and identified by amino acid sequence to be a thaumatin-like protein. The partial sequencing of protein contains 111 aminoacids. The TLP coding gene was sequenced by isolating DNA and amplifying with the specific TLP primers. The 181bp PCR amplified product was sequenced. The comparison of sequence with the other TLP proteins gave 100% similarity. The antimicrobial activity of TLP protein was tested against Candida albicans, Bacillus subtilis, E.coli, Saccharomyces cerevisiae as they are pathogenic organisms. The results showed that it has maximum inhibitory affect against Candida albicans.

Download