Partial purification and characterisation of polyphenol oxidase and peroxidase from marula fruit ( subsp. Caffra)

摘要: Abstract Marula fruit, native to sub-Saharan Africa, is of growing commercially importance. Polyphenol oxidase (PPO) and peroxidase from the fruit were partially purified by a combination temperature induced phase separation in Triton X-114, DEAE-ion exchange Sephadex G100 gel filtration. PPO activity was 58-fold with 75% recovery while purification factor for 19% 25% recovery. The enzymes characterised enzyme concentration–reaction rate relationship, thermal stability, pH molecular weight, isoelectric point (pI) kinetic parameters. shared same weight (71 kDa) pI (5.43). Thermal deactivation curves bi-phasic both activities. Peroxidase displayed maximal at 4.0 ABTS (2,2′-azino-(bis-3-ethylbenzthiazoline-6-sulfonic acid)) K M 1.77 mM hydrogen peroxide. optimum 7.0 catechol. had values 1.41, 1.43, 3.73 4.99 catechin, 4-methylcatechol, 3,4-dihydroxyphenylpropanoic acid (DHPPA) catechol, respectively.