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: This procedure resulted in 74.57 fold purification and recovery of 5.02%. Molecular mass of the purified enzyme was found to be 224 kDa, while subunit molecular mass of 45 kDa was adjudged using gel electrophoresis suggesting its pentameric nature. Bromelain treatment inactivated the enzyme by 11.5%; sodium hexmetaphosphate, L-glutamate and 1,2-cyclohexylenedinitrilotetraacetic acid could inhibit enzyme activity by ~40%; while ethylenediamine tetraacetic acid caused 58.1% inhibition. Papain, pepsin, histidine and DL-malic acid did not have any discernable effect on its activity.

Purification and characterization of Limonoate-D-ring lactone hydrolase from kinnow fruits grown in Punjab, India