期刊
PHARMACEUTICAL BIOLOGY
卷 60, 期 1, 页码 308-318出版社
TAYLOR & FRANCIS LTD
DOI: 10.1080/13880209.2022.2032208
关键词
Waste product; RSM; Alcalase(R); antioxidant
资金
- National Research Council of Thailand (NRCT) [PHD61I0037]
This study optimized the hydrolysis reaction catalyzed by Alcalase(R) to generate sericin hydrolysates with antioxidant activity, and found that temperature played a major role in the scavenging capacity of the hydrolysates.
Context: Sericin, a protein found in wastewater from the silk industry, was shown to contain a variety of biological activities, including antioxidant. The enzymatic conditions have been continuously modified to improve antioxidant effect and scavenging capacity against various free radicals of silk sericin protein. Objective: Variables in enzymatic reactions, including pH, temperature and enzyme/substrate ratio were analysed to discover the optimum conditions for antioxidant activity of sericin hydrolysates. Materials and methods: Hydrolysis reaction catalysed by Alcalase(R) was optimized through response surface methodology (RSM) in order to generate sericin hydrolysates possessing potency for % inhibition on 2,2-diphenyl-1-picrylhydrazyl (DPPH) radicals, ferric-reducing power and peroxyl scavenging capacity. Flow cytometry was performed to evaluate cellular ROS level in human HaCaT keratinocytes and melanin-generating MNT1 cells pre-treated either with 20 mg/mL RSM-optimized sericin hydrolysates or 5 mM N-acetyl cysteine (NAC) for 60 min prior exposure with 1 mM hydrogen peroxide (H2O2). Results: Among these three variables, response surface plots demonstrate the major role of temperature on scavenging capacity of sericin hydrolysates. Sericin hydrolysates prepared by using Alcalase(R) at RSM-optimized condition (enzyme/substrate ratio: 1.5, pH: 7.5, temperature: 70 degrees C) possessed % inhibition against H2O2 at 99.11 +/- 0.54% and 73.25 +/- 8.32% in HaCaT and MNT1 cells, respectively, while pre-treatment with NAC indicated the % inhibition only at 30.26 +/- 7.62% in HaCaT and 51.05 +/- 7.14% in MNT1 cells. Discussion and conclusions: The acquired RSM information would be of benefit for further developing antioxidant peptide from diverse resources, especially the recycling of waste products from silk industry.
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