BACKGROUND: The extraction, purification, and characterisation of peroxidase (POD) and @entity3978 oxidase ( @entity20179 ) were studied for Kalipatti sapota fruit. The crude enzyme extract was partially purified by @entity1329 precipitation followed by BioGel P100 size exclusion and Unosphere Q anion-exchange chromatography. RESULTS: Molecular weights of 20 kDa (POD) and 24 kDa ( @entity20179 ) were indicated by @entity214 -PAGE. A single band was observed on @entity214 -PAGE with a fold purity of 10.38 and 7.42 for POD and @entity20179 , respectively. Michaelis-Menten constants for POD and @entity20179 were 22.3 and 23.0   mmol   L(-1) using @entity12682 and @entity6153 as substrates. Thermal inactivation kinetics was studied in the temperature range of 60-95     C. The crude extract of POD and @entity20179 showed D-values of 2.2-60.2 and 1.0-35.2   min; Z-values of 18.7        0.4 and 16.0        0.3     C; and activation energies (Ea ) of 128.6 and 151.0 kJ mol(-1) , respectively. CONCLUSION: POD and @entity20179 showed good stability over a wide range of pH and temperature. As reflected by Z and Ea values, the fruit matrix had no significant influence towards enzyme stability. Designing of thermal process should take into consideration D- and Z-values of the enzymes along with D- and Z-values of microorganisms to obtain a product with better shelf life.    2017 Society of Chemical Industry.

Partial purification, characterisation and thermal inactivation kinetics of peroxidase and XXXX oxidase isolated from Kalipatti sapota (Manilkara zapota).

@entity3978 :: ('CHEBI:26195', 'Chemical') :: ['polyphenol'] @entity20179 :: ('5498', 'Gene') :: ['PPO'] @entity12682 :: ('MESH:D006139', 'Chemical') :: ['guaiacol'] @entity1329 :: ('MESH:D000645', 'Chemical') :: ['ammonium sulfate'] @entity214 :: ('CHEBI:8984', 'Chemical') :: ['SDS'] @entity6153 :: ('MESH:C034221', 'Chemical') :: ['catechol']
@entity3978 :: (CHEBI:26195,Chemical) :: ['polyphenol']
