gamma-Tocopherol methyltransferase (gamma-TMT) (EC 2.1.1.95) is the last enzyme in the tocopherol biosynthetic pathway and it catalyzes the conversion of gamma-tocopherol into alpha-tocopherol, the nutritionally significant and most bioactive form of vitamin E. Although the gamma-TIVIT gene has been successfully overexpressed in many crops to enhance their alpha-tocopherol content but still only few attempts have been made to uncover its structural, functional and regulation aspects at protein level. In this study, we have cloned the complete 909bp coding sequence of Glycine max gamma-TMT (Gm gamma-TMT) gene that encodes the corresponding protein comprising of 302 amino acid residues. The deduced Gin gamma-TMT protein showed 74-87% sequence identity with other characterized plant gamma-TMTs. Gm gamma-TMT belongs to Class I Methyl Transferases that have a Rossmann-like fold which consists of a seven-stranded p sheet joined by a helices. Heterologous expression of Gm gamma-TMT in pET29 alpha expression vector under the control of bacteriophage T7 promoter produced a 37.9 kDa recombinant Gm gamma-TMT protein with histidine hexamer tag at its C-terminus. The expression of recombinant Gm gamma-TMT protein was confirmed by western blotting using anti His antibody. The recombinant protein was purified by Ni2+-NTA column chromatography. The purified protein showed SAM dependent methyltransferase activity. The alpha-tocopherol produced in the in-vitro reaction catalyzed by the purified enzyme was detected using reverse phase HPLC. This study has laid the foundation to unveil the biochemical understanding of Gm gamma-TMT enzyme which can be further explored by studying its kinetic behaviour, substrate specificity and its interaction with other biomolecules. (C) 2017 Elsevier Inc. All rights reserved.