1. Peroxidase from jackfruit has been purified, characterized and studied for its thermal inactivation.
2. The enzyme showed maximum activity at pH 5.5 and 55-60°C, and was inhibited by Ca2+, glutathione, cysteine and ascorbic acid.
3. Heat treatment caused a decrease in the POD activity, antioxidative activity and total phenolics in jackfruit extracts.
This article provides an overview of the purification, characterization and thermal inactivation of peroxidase (POD) from jackfruit bulbs. The authors provide detailed information on the purification process, enzyme properties such as molecular weight, optimal pH and temperature, heat inactivation kinetics and thermodynamic parameters, kinetic parameters and substrate specificity of POD, effects of metal ions and food additives on POD activity, chemical modification of POD, preparation of jackfruit extracts and heat treatment, ferric-reducing antioxidant power (FRAP), ABTS radical scavenging ability and total phenolics content of jackfruit extract.
The article is generally reliable with regards to its scientific content; however there are some potential biases that should be noted. Firstly, the authors do not discuss any possible risks associated with the use of POD or its thermal inactivation; this could be important to consider when designing food processing methods using this enzyme. Secondly, the authors do not explore any counterarguments or present both sides equally; they focus solely on the positive aspects of their findings without considering any potential drawbacks or limitations to their research. Finally, there is a lack of evidence provided for some claims made throughout the article; for example when discussing the effects of metal ions on POD activity it would be beneficial to include data or figures to support these claims.
In conclusion, this article provides a comprehensive overview of peroxidase from jackfruit bulbs but there are some potential biases that should be noted when assessing its trustworthiness and reliability.