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Iron-Binding Capacity and Antidiabetic Activity of Baby Clam (Corbiculidae sp.) Meat Protein Hydrolysate Vo, Tam Dinh Le; Huynh, Thu; Le, Thuy Thi; Tran, An Thi Tuong; Vo, Bao Chi
Indonesian Journal of Chemistry Vol 25, No 1 (2025)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.22146/ijc.98947

Abstract

Baby clam (Corbiculidae sp.) meat is served as a traditional dish in Vietnam, and the antioxidant activity of its protein extract has been discovered. This study evaluates baby clam meat protein hydrolysate's iron-binding capacity (IBC) and antidiabetic activity. Initially, an analysis of the basic chemical composition of the meat was conducted. Subsequently, Alcalase was employed for hydrolysis. The highest IBC and α-amylase inhibition activity were targets for obtaining the best hydrolysis condition, including the clam meat-to-water ratio, enzyme-to-substrate (E:S) ratio, and time. Under the best condition, the hydrolysates demonstrated the IBC of 1246.20 ± 44.00 µg Fe2+/g protein and α-amylase inhibition activity of 48.33 ± 1.44%, approaching three-quarters of the activity of ethylenediaminetetraacetic acid (EDTA) sodium salt and acarbose, respectively. These results served as preliminary data for the development of the protein hydrolysates as a natural iron chelator or α-amylase inhibitor, which could support the treatment of iron deficiency and diabetes.
Study on Zinc-binding Capacity of Featherback (Chitala ornata) Skin Hydrolysate Vo, Tam Dinh Le; Tran, Thinh Ngoc; Vo, Bao Chi; Ma, Hieu Trung; Tran, Hoa Gia; Nguyen, Son Manh; Hoang, Quyen Phuong; Nguyen, Van Thi Tuyet; Nguyen, Mai Thi Ngoc; Nguyen, Thao Huynh Ngoc; Pham, Vy Thuy; Cao, Khang Tran Gia; Pham, Cuong Viet
Indonesian Journal of Chemistry Vol 25, No 2 (2025)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.22146/ijc.98948

Abstract

This study aims to valorize featherback (Chitala ornata) skin by-product by generating zinc-binding hydrolysate using Alcalase. Commencing with an effective assessment of hydrolysis conditions on the zinc-binding capacity (ZnBC), the hydrolysate gave the highest ZnBC. Subsequently, the hydrolysate was fractionated using ultrafiltration centrifugal devices, analyzed for its amino acid composition, and examined for the stability of its ZnBC against heat and pH. At the best hydrolysis condition, including the skin:water ratio of 1:4 (w/v), enzyme:substrate (E:S) ratio of 40 U/g protein, pH = 8, temperature of 50 °C, and hydrolysis time of 5 h, the gained hydrolysate exhibited the greatest ZnBC of 30.28 ± 0.83% (2.66 folds lower than that of ethylenediamine tetraacetic acid disodium salt (Na2EDTA)) and contained 8 essential amino acids (making 21.12% total amino acids). Besides, the hydrolysate’s ZnBC could retain above 66% after pH treatment in range 1–11 or thermal treatment at 100 °C for 180 min. The < 1 kDa fraction expressed the highest ZnBC of 38.48 ± 2.96%, 2.09 times lower than Na2EDTA. These findings indicate that hydrolysate and/or its peptide fractions derived from featherback skin could be a natural supplement, especially when producing functional food or nutraceuticals.