TH. PREMILA DEVI AND L.R. SINGH
Abstract
Bromelain, a cysteine proteinase which is having a wide range of application was purified by immunoaffinity chromatography using polyclonal antibody raised against pineapple stern bromelain from pineapple crown leaf. The crude enzyme preparation was subjected to ammonium sulphate fractionation and then subjected to immunoaffinity chromatography. The purified enzyme was found to be homogeneous at 12% acrylamide. 23.1 units of the pure enzyme could be recovered from pineapple crown leaf which is otherwise thrown away as waste causing environmental pollution.