Optimization of hydrolysis conditions for the production of protein hydrolysates from fish wastes using response surface methodology

Korkmaz, Koray; Tokur, Bahar

doi:10.1016/j.fbio.2021.101312

Cited by 36 publications

(22 citation statements)

References 38 publications

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“…According to the single-factor experiment results, response surface methodology was employed to estimate the influence of independent variables ( X 1 , pH; X 2 , enzyme dose; and X 3 , temperature) on ACEi activity ( 47 – 49 ). The three levels ( X 1 : 6.5, 7.0, and 7.5; X 2 : 50, 55, and 60°C; X 3 : 1.0, 1.5, and 2.0%) of the Box-Behnken design were designed to analyze the effects of three variables on ACEi activity.…”

Section: Methodsmentioning

confidence: 99%

Preparation, Characterization, and Cytoprotective Effects on HUVECs of Fourteen Novel Angiotensin-I-Converting Enzyme Inhibitory Peptides From Protein Hydrolysate of Tuna Processing By-Products

et al. 2022

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To effectively utilize skipjack tuna (Katsuwonus pelamis) processing by-products to prepare peptides with high angiotensin-I-converting enzyme (ACE) inhibitory (ACEi) activity, Neutrase was selected from five kinds of protease for hydrolyzing skipjack tuna dark muscle, and its best hydrolysis conditions were optimized as enzyme dose of 1.6%, pH 6.7, and temperature of 50°C using single factor and response surface experiments. Subsequently, 14 novel ACEi peptides were prepared from the high ACEi protein hydrolysate and identified as TE, AG, MWN, MEKS, VK, MQR, MKKS, VKRT, IPK, YNY, LPRS, FEK, IRR, and WERGE. MWN, MEKS, MKKS, and LPRS displayed significantly ACEi activity with IC50 values of 0.328 ± 0.035, 0.527 ± 0.030, 0.269 ± 0.006, and 0.495 ± 0.024 mg/mL, respectively. Furthermore, LPRS showed the highest increasing ability on nitric oxide (NO) production among four ACEi peptides combining the direct increase and reversing the negative influence of norepinephrine (NE), and MKKS showed the highest ability on directly decreasing and reversing the side effects of NE on the secretion level of endothelin-1 (ET-1) among four ACEi peptides. These findings demonstrate that seafood by-product proteins are potential ACEi peptide sources and prepared ACEi peptides from skipjack tuna dark muscle, which are beneficial components for functional food against hypertension and cardiovascular diseases.

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Section: Methodsmentioning

confidence: 99%

Preparation, Characterization, and Cytoprotective Effects on HUVECs of Fourteen Novel Angiotensin-I-Converting Enzyme Inhibitory Peptides From Protein Hydrolysate of Tuna Processing By-Products

et al. 2022

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“…According to the single-factor experiment results, a response surface methodology was employed to estimate the influence of independent variables ( X 1 , pH; X 2 , temperature; X 3 , enzyme dose) in glycine-sodium hydroxide buffer (0.05 M) on ACEi activity [ 62 , 63 ]. The Box–Behnken design of three levels ( X 1 : 9, 9.5, and 10; X 2 : 50, 55, and 60 °C; X 3 : 1.5, 2.0, and 2.5%) was used to analyze the effects of three variables on ACEi activity.…”

Section: Methodsmentioning

confidence: 99%

Preparation, Identification, Molecular Docking Study and Protective Function on HUVECs of Novel ACE Inhibitory Peptides from Protein Hydrolysate of Skipjack Tuna Muscle

et al. 2022

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To prepare bioactive peptides with high angiotensin-I-converting enzyme (ACE)-inhibitory (ACEi) activity, Alcalase was selected from five kinds of protease for hydrolyzing Skipjack tuna (Katsuwonus pelamis) muscle, and its best hydrolysis conditions were optimized using single factor and response surface experiments. Then, the high ACEi protein hydrolysate (TMPH) of skipjack tuna muscle was prepared using Alcalase under the optimum conditions of enzyme dose 2.3%, enzymolysis temperature 56.2 °C, and pH 9.4, and its ACEi activity reached 72.71% at 1.0 mg/mL. Subsequently, six novel ACEi peptides were prepared from TMPH using ultrafiltration and chromatography methods and were identified as Ser-Pro (SP), Val-Asp-Arg-Tyr-Phe (VDRYF), Val-His-Gly-Val-Val (VHGVV), Tyr-Glu (YE), Phe-Glu-Met (FEM), and Phe-Trp-Arg-Val (FWRV), with molecular weights of 202.3, 698.9, 509.7, 310.4, 425.6, and 606.8 Da, respectively. SP and VDRYF displayed noticeable ACEi activity, with IC50 values of 0.06 ± 0.01 and 0.28 ± 0.03 mg/mL, respectively. Molecular docking analysis illustrated that the high ACEi activity of SP and VDRYF was attributed to effective interaction with the active sites/pockets of ACE by hydrogen bonding, electrostatic force, and hydrophobic interaction. Furthermore, SP and VDRYF could significantly up-regulate nitric oxide (NO) production and down-regulate endothelin-1 (ET-1) secretion in HUVECs after 24 h treatment, but also abolish the negative effect of 0.5 μM norepinephrine (NE) on the generation of NO and ET-1. Therefore, ACEi peptides derived from skipjack tuna (K. pelamis) muscle, especially SP and VDRYF, are beneficial components for functional food against hypertension and cardiovascular diseases.

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“…Enzymatic hydrolysis and optimization values of trout, whiting, and anchovy by‐products in the present study were performed according to our previous publication (Korkmaz & Tokur, 2021).…”

Section: Methodsmentioning

confidence: 99%

Investigation of the quality parameters of hydrolysates obtained from fish by‐products using response surface methodology

Korkmaz

Tokur

2022

Food Processing Preservation

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Fish protein hydrolysates (FPH), which comprise a combination of small protein or peptide and free amino acids, may be suitable for use in a variety of applications. For this purpose, the hydrolysis process was carried out for the by-products of trout, whiting, and anchovy with alkaline protease, protamex, and flavourzyme, and the quality of the protein hydrolysate generated under optimized conditions was determined by proximate compositions, amino acid contents, heavy metal, and trace element levels and peptide molecular weight sizes. The time, temperature, and enzyme proportions were determined according to the hydrolysis degree (DH%) under optimum conditions identified by response surface methodology (RSM). The crude protein, lipid, and ash contents of trout, whiting, and anchovy by-products hydrolysates ranged from 77.03% to 88.54%, 3.28% to 6.12%, and 8.18% to 16.8% for dry matter, respectively.Considering the total amino acid contents, the highest number of amino acids was aspartic and glutamic acid in all fish and enzyme groups. In terms of essential amino acids, the highest concentrations of cystine, histidine, lysine, and methionine were found in anchovy by-product hydrolysates produced using the flavourzyme. Using FAO/WHO reference protein as a base, lysine was found to have the highest chemical score for trout by-products hydrolysates using protamex (85.14%), whiting byproducts hydrolysates using alkaline protease (83.66%), and anchovies by-products hydrolysates using flavourzyme (88.45%). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis revealed that the electrophoresis pattern of the hydrolysates of trout, whiting, and anchovy by-products optimized with the RSM using alkaline protease, protamex, and flavourzyme enzymes showed variations depending on the enzyme type and fish by-products.

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Optimization of hydrolysis conditions for the production of protein hydrolysates from fish wastes using response surface methodology

Cited by 36 publications

References 38 publications

Preparation, Characterization, and Cytoprotective Effects on HUVECs of Fourteen Novel Angiotensin-I-Converting Enzyme Inhibitory Peptides From Protein Hydrolysate of Tuna Processing By-Products

Preparation, Characterization, and Cytoprotective Effects on HUVECs of Fourteen Novel Angiotensin-I-Converting Enzyme Inhibitory Peptides From Protein Hydrolysate of Tuna Processing By-Products

Preparation, Identification, Molecular Docking Study and Protective Function on HUVECs of Novel ACE Inhibitory Peptides from Protein Hydrolysate of Skipjack Tuna Muscle

Investigation of the quality parameters of hydrolysates obtained from fish by‐products using response surface methodology

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