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POTENTIALITY OF PROTEIN HYDROLYSATE FROM ANADARA GRANOSA AS NUTRACEUTICAL AGENT: ANTIOXIDANT AND ANTIBACTERIAL ACTIVITIES

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Objective: This study aims to extract protein hydrolysate from Anadara granosa and assess its impact on protein solubility, antioxidant, and antibacterial activities. Methods: Several methods were used, including the isolation of enzyme bromelain, protein extraction from A. granosa, and the breakdown of protein using trypsin and bromelain. Together with its protein solubility, antioxidant activity (IC50) against free radicals (DPPH), the protein hydrolysate's antibacterial activity (MIC and inhibition zone) against Staphylococcus aureus and Escherichia coli was evaluated. Results: With a molecular weight of 10 kDa and an IC50 of 83.81 mg/ml, the trypsin protein hydrolysate fraction showed remarkable antioxidant activity after 5 h of incubation. At a dosage of just 0.25 mg/ml, the A. granosa protein and its corresponding hydrolysate had inhibitory zones against S. aureus and E. coli that were comparable to those observed in samples treated with amoxicillin. Using trypsin as an enzyme for 3 or 5 h produced the strongest hydrolyzed product. The trypsin hydrolysate was better than the bromelain hydrolysate because of its antioxidant and antibacterial activities. Conclusion: Based on the results, antioxidant and antibacterial activities, and protein solubility were influenced by enzymatic hydrolysis.
Title: POTENTIALITY OF PROTEIN HYDROLYSATE FROM ANADARA GRANOSA AS NUTRACEUTICAL AGENT: ANTIOXIDANT AND ANTIBACTERIAL ACTIVITIES
Description:
Objective: This study aims to extract protein hydrolysate from Anadara granosa and assess its impact on protein solubility, antioxidant, and antibacterial activities.
Methods: Several methods were used, including the isolation of enzyme bromelain, protein extraction from A.
granosa, and the breakdown of protein using trypsin and bromelain.
Together with its protein solubility, antioxidant activity (IC50) against free radicals (DPPH), the protein hydrolysate's antibacterial activity (MIC and inhibition zone) against Staphylococcus aureus and Escherichia coli was evaluated.
Results: With a molecular weight of 10 kDa and an IC50 of 83.
81 mg/ml, the trypsin protein hydrolysate fraction showed remarkable antioxidant activity after 5 h of incubation.
At a dosage of just 0.
25 mg/ml, the A.
granosa protein and its corresponding hydrolysate had inhibitory zones against S.
aureus and E.
coli that were comparable to those observed in samples treated with amoxicillin.
Using trypsin as an enzyme for 3 or 5 h produced the strongest hydrolyzed product.
The trypsin hydrolysate was better than the bromelain hydrolysate because of its antioxidant and antibacterial activities.
Conclusion: Based on the results, antioxidant and antibacterial activities, and protein solubility were influenced by enzymatic hydrolysis.

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