Biochemical properties of purified polyphenol oxidase from bitter leaf ().

Polyphenol oxidase which is responsible for oxidative conversion of phenolic compounds to polymers, has continued to attract the attention of scientists. Here, we report the extraction, purification and biochemical properties of polyphenol oxidase (PPO) from bitter leaf (). The enzyme was purified and concentrated using a non-conventional approach, aqueous two-phase partitioning (ATPS) and the biochemical properties of the purified enzyme were investigated.

Potentials of purified tyrosinase from yam ( spp) as a biocatalyst in the synthesis of cross-linked protein networks.

We report the usefulness of yam tyrosinase as a catalyst in the synthesis of cross-linked protein networks for biopolymers. The enzyme was purified using aqueous two-phase partitioning (ATPs) and peptide mapping on SDS-PAGE was carried out to ascertain degree of similarities of tyrosinase from the yam species. The mapping revealed distinct peptide bands of 3, 4, 4 and 2 for tyrosinase from , , and respectively purified using conventional method.