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Abstract Background and objective: PPO enzyme catalyze oxidation of o-diphenol to o-quinone by utilizing oxygen and the final product is undesirable black pigments. Fruits and vegetables are sensitive to enzymatic browning. Several industries produce wastewater containing phenol and its derivatives. Removal of phenols and degradation from wastewater by using enzymes is possible by developing biosensors to detect phenolic compounds. The inhibition of PPO is significant for the preservation of food products, vegetables with good quality and also clinically useful for the treatment of dermatological disorders related to hyperpigmentation also helpful in developing cosmetic products. In view of the applications the present investigation deals with the characterization and inhibition kinetics of PPO from Cinnamomum verum fruit coat. Material and methods: Purification and quantification of an enzyme are done by ammonium sulfate precipitation, dialysis and followed by the sephadex G-100 column chromatography technique. Molecular weight was analyzed by SDS-PAGE. The Km and Vmax were determined from a Lineweaver-Burk plot by following the optimum pH, temperature and freeze-thaw conditions. The effect of

Abstract Background Higher aldehyde dehydrogenases (ALDH) activity is one of the important signatures of breast cancer appearance and has been associated with poor prognosis. ALDH1A3 has been over-expressed in breast cancer patients. This study aims to analyze gene expression patterns of 18 ALDH isozymes in breast cancer tissue samples. It is carried out using a chip-based microarray, next-generation DNA sequencing of ALDH2 gene following in silico study to identify the natural products which act as inhibitors for over-expressed ALDH isoforms. The synthesis of rutin-copper complex and cell viability assay is carried out on MDA-MB-468 cell line. Results ALDH1A3 and ALDH18A1 have shown the highest positive mean fold of variation; whereas, ALDH2 and ALDH1A2 have shown the highest negative mean fold variation. In silico studies revealed that rutin has the highest binding affinity with both ALDH1A3 and ALDH18A1 and supported with IC50 value of rutin against MDA-MB-468 cells (144.50 μg/ml). Chemically synthesized rutin-copper complex significantly lowered the IC50 value to 119.40 μg/ml. The next-generation sequencing study provides the novel single nucleotide polymorphism (SNP) from T to G in the ALDH2 gene. Conclusion The present study signifies that, along with ALDH1A3, ALDH18A1 also acts as a marker for breast cancer. Apart from that, inhibitors of ALDH1A3 and ALDH18A1 were attained. Perhaps the single nucleotide polymorphism (SNP) obtained during the mutation analysis may be the probable cause of the highest downregulation of ALDH2 in breast cancer.