Bovine Bone Gelatin Research Articles

Formation, characterization of gelatine from the scales of Labeo rohita and its comparison with bovine bone gelatine

The study isolated gelatin from Labeo rohita scales and characterized it using Fourier transform infrared spectroscopy (FTIR), X-Ray diffraction (XRD), and scanning electron microscopy (SEM). The resulting gelatine and commercial bovine bone gelatin were found to have crystalline structures, with both being porous and spherical. L. rohita scales yielded 5.45 % of gelatin. The moisture content varied between 11.12 % and 9.02 % for the gelatin, while the ash content varied between 2.17 % and 2.36 %. The protein content was 82.78 % in the fish scales gelatin, while the commercial bovine bone gelatin had 94.27 %. The fat content of gelatin isolated from scales of L. rohita was 1.21 %, whereas fat in commercial bovine bone gelatin was 1.19 %. The fiber contents of gelatin isolated from fish scales was 0.44 % while fiber content of commercial bovine bone gelatin was 0.65 %. The study confirms the high-quality gelatin-bearing characteristics of fish scales, suggesting that it can be produced for various purposes and potentially increase the economic value of fish. The isolated gelatin from fish by-products could also be a valuable resource.

Synthesis and Characterization of Hybridfiber from Gelatin Modified by PVACOS Using Coaxial Electrospinning Techniques as an Advanced Medical Textile Material

The synthesis of hybrid fiber based on bovine bone gelatin combined with polyvinyl alcohol-chitosan-oxidized sucrose (PVACOS) has been successfully carried out using the coaxial electrospinning technique. The presence of oxidized sucrose can improve the diameter and the tensile strength of hybrid fibers due to the formation of new covalent bonds. The combination of gelatin with PVACOS material aims to increase the strength of the hybrid fiber so that it has better tensile strength characteristics and improves the diameter of the resulting hybrid fiber. The characterization of the resulting material was tested using FTIR, SEM, EDX, XRD, and TGA. Based on FTIR analysis, there is an increase in absorption intensity in the 2900 cm-1 – 3000 cm-1 band, which indicates the occurrence of covalent bond interactions so that it can increase the bond strength between materials with the performance of crystalline materials. Apart from that, the morphological structure of the hybrid fibers was also investigated using scanning electron microscopy (SEM), and the resulting fiber diameter for Ge-Ch, Ge-Ch-PVA, Ge-PVACOS 3%, and Ge-PVACOS 5%, respectively, was 0.4049 µm. 0.3735 µm, 0.3388 µm, and 0.3206 µm. The tensile strengths of hybrid fiber for Ge-PVACOS 3% and Ge-PVACOS 5%, respectively, are 39.91935 N/m2 and 76.12507 N/m2. Statistical tests show that the concentration of oxidized sucrose has a significant influence on hybrid fiber performance. The significance values for diameter and tensile strength are 0.0486 and 0.0325, respectively. According to this performance, the Ge-PVACOS hybrid fiber is recommended as a material for advanced medical textiles. Doi: 10.28991/ESJ-2024-08-02-022 Full Text: PDF

Fish oil encapsulation by genipin-crosslinked complex coacervation between gelatin and different anionic polysaccharides

Herein, a combination approach of bovine bone gelatin (BBG)/anionic polysaccharide (AP) complex coacervation with genipin crosslinking was developed to successfully fabricate fish oil-loaded genipin-crosslinked BBG/AP (fish oil@BBG-genipin-AP) powders. The genipin crosslinking process promoted the formation of larger fish oil@BBG-genipin-AP particles from the BBG/AP particles and fish oil@BBG/AP particles. AP types (gum Arabic, GA; sodium alginate, SA; sodium carboxymethyl cellulose, CMC) and concentrations significantly affected the critical pH to form complex coacervated particles, the powder physicochemical properties, the powder oxidative stability, and the powder in vitro digestion. The fish oil@BBG-genipin-CMC powder at the CMC preparation concentration of 17.5 mg/mL showed the highest loading capacity value (44.3% ± 0.8%), almost the highest encapsulation efficiency value (90.9% ± 0.7%), and the highest encapsulation yield (91.3% ± 2.0%). Due to the environmental pH change, the powders changed to emulsion droplets in the gastric phase and then released free fatty acids in the small intestinal phase. The highest FFA release percentages after the gastrointestinal phase (2 h in the gastric phase and 2 h in the small intestinal phase) were dependent on both AP types and their concentrations (GA: 64.8 ± 2.9%, 62.5 mg/mL; SA: 55.0 ± 3.1%, 15 mg/mL; and CMC: 48.9 ± 1.5%, 12.5 mg/mL). GA at a concentration of 62.5 mg/mL might be the best system to prepare fish oil@gelatin-genipin-anionic polysaccharide powders for fish oil digestion. This work provided useful information to develop oil-encapsulation powders for functional foods and understand the influences of wall materials on the fabrication and properties of powder foods.

Effects of polyphenol and gelatin types on the physicochemical properties and emulsion stabilization of polyphenol-crosslinked gelatin conjugates

Herein, six types of polyphenol-crosslinked gelatin conjugates (PGCs) with ≥ two gelatin molecules were prepared using a covalent crosslinking method with two types of polyphenols (tannic acid and caffeic acid) and three types of gelatins (bovine bone gelatin, cold water fish skin gelatin, and porcine skin gelatin) for the emulsion stabilization. The structural and functional properties of the PGCs were dependent on both polyphenol and gelatin types. The storage stability of the conjugate-stabilized emulsions was dependent on the polyphenol crosslinking, NaCl addition, and heating pretreatment. In particular, NaCl addition promoted the liquid-gel transition of the emulsions: 0.2 mol/L > 0.1 mol/L > 0.0 mol/L. Moreover, NaCl addition also increased the creaming stability of the emulsions stabilized by PGCs except tannic acid-crosslinked bovine bone gelatin conjugate. All the results provided useful knowledge on the effects of molecular modification and physical processing on the properties of gelatins.

Two types of pH-responsive genipin-crosslinked gelatin conjugates with high surface hydrophobicity for emulsion stabilization

The development of genipin modification methods has attracted much attention to improve the functional properties of proteins in the fields of food science. In this work, two types of pH-responsive genipin-crosslinked bovine bone gelatin conjugates with high surface hydrophobicity were developed for emulsion stabilization. One was genipin molecule-crosslinked gelatin conjugates prepared at acidic pH and the other was genipin macromer-crosslinked gelatin conjugates prepared at neutral and basic pH. The degrees of crosslinking increased with the increase of preparation pH. They increased with the increase of genipin-to-gelatin mass ratios at acidic pH, whereas decreased with the increase of genipin-to-gelatin mass ratios at neutral and basic pH. The surface hydrophobicity values, molecular weights, and emulsifying properties (creaming stability, emulsion activity index, and emulsion stability index) of the obtained conjugates increased with the increase of both preparation pH and genipin-to-gelatin mass ratios. This work provided useful knowledge to understand how the preparation parameters (preparation pH and genipin-to-gelatin mass ratio) and genipin structures (molecule and macromer) affect a protein's degrees of crosslinking, physicochemical properties, and emulsifying properties.

Effect of molecular weight distributions on the gelation rate and other physicochemical properties of bovine bone gelatin (Type B)

The physicochemical properties of bovine bone gelatins (Type B) including amino acid and subunit compositions, gelation rate, Bloom values, viscosity, dynamic storage modulus (G’), gelling and melting temperature were investigated comparatively on the basis of molecular weight distributions (MWD). The MWD of gelatin was divided into three segments: >1000 kDa (H), 130 kDa–1000 kDa (M), and <130 kDa (L) for quantitative description and analysis. Results showed similar amino acid compositions for gelatins across different MWD. Gelatins with similar Bloom values exhibited different MWD, whose gelation rate increased with increasing segment H content and decreasing segment M and L content. Viscosity of gelatin was positively correlated with segment H content, and their gelling and melting temperature exhibited little difference. The present study suggests that increasing segment H content or decreasing segment M and L content in gelatin samples can increase the gelation rate and viscosity, making it suitable for 3D food printing.

Effects of Long-Term Administration of Bovine Bone Gelatin Peptides on Myocardial Hypertrophy in Spontaneously Hypertensive Rats.

The research purpose was to investigate the effects and the underlying molecular mechanisms of bovine bone gelatin peptides (BGP) on myocardial hypertrophy in spontaneously hypertensive rats (SHR). BGP relieved myocardial hypertrophy and fibrosis in SHR rats in a dose-dependent manner by reducing the left ventricular mass index, myocardial cell diameter, myocardial fibrosis area, and levels of myocardial hypertrophy markers (atrial natriuretic and brain natriuretic peptide). Label-free quantitative proteomics analysis showed that long-term administration of BGP changed the left ventricle proteomes of SHR. The 37 differentially expressed proteins in the high-dose BGP group participated in multiple signaling pathways associated with cardiac hypertrophy and fibrosis indicating that BGP could play a cardioprotective effect on SHR rats by targeting multiple signaling pathways. Further validation experiments showed that a high dose of BGP inhibited the expression of phosphoinositide 3-kinase (Pi3k), phosphorylated protein kinase B (p-Akt), and transforming growth factor-beta 1 (TGF-β1) in the myocardial tissue of SHR rats. Together, BGP could be an effective candidate for functional nutritional supplements to inhibit myocardial hypertrophy and fibrosis by negatively regulating the TGF-β1 and Pi3k/Akt signaling pathways.

Preparation of food-grade EDC/NHS-crosslinked gelatin nanoparticles and their application for Pickering emulsion stabilization

Herein, a safe desolvation and crosslinking method was developed to prepare food-grade bovine bone gelatin (BBG) nanoparticles for Pickering emulsion stabilization. The nanoparticle-like structures were formed by adjusting pH 9.0 and adding ethanol, and then stable nanoparticles were formed by using N-(3-dimethylaminopropyl)-N′-ethylcarbodiimide (EDC) and N-hydroxysuccinimide (NHS) as crosslinker. Compared with other pH (2.5, 5.0, 7.0, and 12.0), pH 9.0 was the appropriate pH to prepare BBG nanoparticles. Individual nanoparticles (6.50 nm in height), oligomeric nanoparticles (13.42–22.52 nm in height), and polymeric nanoparticles (obvious liquid-precipitate separation) were formed at EDC·HCl/NHS concentrations of 6, 9–12, and 15–20 mg/mL, respectively. The oligomeric nanoparticles induced the highest emulsion creaming stability. The emulsion creaming ability increased with the increase of BBG nanoparticle concentrations. Low NaCl concentration (e.g., 100 mmol/L) could increase the emulsion creaming stability. Finally, 4 °C was the best storage temperature for fish oil-loaded Pickering emulsions.

Interaction of curcumin with four types of gelatins in nanoparticles: Mechanism and application for emulsion stabilization

The research of the interaction between proteins and functional active substances in the protein nanoparticles is a research hotspot in the field of food science. Gelatin type had a significant effect on the structural and functional properties of gelatins. Herein, the interaction mechanism of curcumin with four types of gelatins (bovine bone gelatin, BBG; cold water fish skin gelatin, CFG; fish gelatin, FG; and porcine skin gelatin, PSG) and the structural and functional properties of gelatin/curcumin nanoparticles were explored. All four types of gelatins could be applied to prepare gelatin/curcumin nanoparticles with an amorphous state of curcumin. The nanoparticle sizes were not dependent on the molecular weight of gelatins. The stability of gelatin/curcumin nanoparticle solutions was dependent not on the nanoparticle size but on the gelatin type. The binding affinity between gelatins and curcumin was dependent on gelatin type and the number of binding sites was nearly 1. The main binding forces to form gelatin-curcumin nanoparticles were hydrogen bonds, Pi-alkyl interaction, and Pi-anion interaction. The nanoparticulation increased the surface hydrophobicity of BBG, FG, and PSG, whereas it decreased the surface hydrophobicity of CFG. The nanoparticulation increased the surface tension of gelatins and decreased the dynamic interfacial tension of gelatins. The functional properties were dependent on both gelatin type and nanoparticulation. CFG/Cur nanoparticulation could not change the creaming stability, whereas other gelatins/curcumin nanoparticulation significantly increased creaming stability than the corresponding gelatins. This work provided the basic knowledge to illustrate the interaction and application of protein nanoparticles for Pickering emulsion stabilization.

Curcumin-encapsulated hydrophilic gelatin nanoparticle to stabilize fish oil-loaded Pickering emulsion

Herein, pH-cycle method was explored to prepare curcumin-encapsulated hydrophilic bovine bone gelatin (BBG/Cur) nanoparticle and then the obtained nanoparticle was applied to stabilize fish oil-loaded Pickering emulsion. The nanoparticle had a high encapsulation efficiency (93.9 ± 0.5 %) and loading capacity (9.4 ± 0.1 %) for curcumin. The nanoparticle-stabilized emulsion had higher emulsifying activity index (25.1 ± 0.9 m2/g) and lower emulsifying stability index (161.5 ± 18.8 min) than BBG-stabilized emulsion. The pH affected the initial droplet sizes and creaming index values of the Pickering emulsions: pH 11.0 < pH 5.0 ≈ pH 7.0 ≈ pH 9.0 < pH 3.0. Curcumin provided obvious antioxidant effect for the emulsions, which was also dependent on pH. The work suggested pH-cycle method could be used to prepare hydrophobic antioxidant-encapsulated hydrophilic protein nanoparticle. It also provided basic information on the development of protein nanoparticles for Pickering emulsion stabilization.

Effects of octenyl succinic anhydride chemical modification and surfactant physical modification of bovine bone gelatin on the stabilization of fish oil-loaded emulsions.

In this work, octenyl succinic anhydride (OSA) chemical modification with surfactant physical modification was combined to modify bovine bone gelatin (BBG) for emulsion stabilization at pH 6.0 (to simulate acidic food environment). OSA modification decreased the β-sheet percentage and increased β-turn percentage of BBG. Further, the combination of OSA modification with surfactant physical modification had obvious and different effects on the emulsifying properties of BBG. The creaming stability of gelatin/surfactant-stabilized emulsions was dependent on gelatin structure, surfactant type, and preparation pH. The emulsions stabilized by OBBG/Span 80 and OBBG/soybean lecithin (only blurry creaming at day 28) had significantly better creaming stability than other emulsions. These results demonstrated that the combination of OSA modification with surfactant modification could be applied to improve the emulsifying properties of BBG.

Karakterisasi Gelatin Hasil Ekstraksi dari Tulang Sapi Melalui Proses Perlakuan Basa NaOH

Gelatin is a soluble protein that acts as a gelling agent and is commonly used as an ingredient in both food and non-food production. Since bone is composed of collagen fibers, it can be used as a raw material for gelatin production. Beef bone is a waste product that is rarely used. Sodium hydroxide (NaOH) can be used as a processing ingredient in the production of type B gelatin because it can remove fats and oils. The purpose of this study was to investigate the effects of 2%, 3%, 4%, 5%, and 6%NaOH concentrations on the properties of bovine bone gelatin at 4 and 6 hours of extraction time. The observed properties were yield, water content, ash content, pH, viscosity, and microbial contamination. The results showed that the pretreatment condition with 6% NaOH and extraction for 6 hours affected the properties of the highest yield, water content dan microbial contamination have fulfilled the SNI. The conclusion of this study is that NaOH can be used in the production of bovine bone gelatin, and there are some advances in producing gelatin with excellent properties for food and non-food applications.

Edible hyaluronic acid-rich burger separator discs prepared from slaughterhouse waste.

In this study, edible films from chicken feet extract (CF), ovine muscle fascia extract (MF), and bovine bone gelatin powder (Gel) were prepared and their characteristics were analyzed. We also used the films as separators of burger cuts and evaluated the organoleptic characteristics of cooked burgers. Hyaluronic acid quantities of CF and MF were measured using colorimetric and spectrophotometry. Results indicated that the concentration of hyaluronic acid in CF (124.11 ppm) was greater than MF (101.11 ppm). The antioxidative property of the CF film (18.47%) was greater than the Gel (1.88%) and MF (Undetectable) films. The CF film was more resistant to water vapor permeability (2.75 × 10−9 g/m.s.pa) than the MF (1.57 × 10−8 g/m.s.pa) and Gel (1.5 × 10−7 g/m.s.pa) films. The Gel film had more appropriate mechanical properties than CF and MF films. The films kept burgers patties independent from one another and prevented them from sticking and freezing together. MF and CF films were able to promote the organoleptic properties of cooked burgers in taste and texture.

Effect of transglutaminase crosslinking on the structural, physicochemical, functional, and emulsion stabilization properties of three types of gelatins

Molecular modification has attracted many attentions in the field of gelatin science. In this work, a transglutaminase (TG) modification method was developed and applied to modify bovine bone gelatin, porcine skin gelatin, and cold-water fish skin gelatin, and then the effect of TG crosslinking on the structural, physicochemical, functional, and emulsion stabilization properties of three types of gelatins were explored and compared. The results demonstrated that TG modification increased the nanoparticle formation behaviors and change the physicochemical and functional properties of three types of gelatins. Further, TG-modified aquatic gelatin showed comparable foaming properties (147% ± 6% for foaming capability and 55% ± 4% for foam stability) and higher emulsifying properties (18 ± 1 m2/g for emulsion activity index and 142 ± 11 min for emulsion stability index) to unmodified mammalian gelatins. In addition, TG-modified gelatins decreased the droplet sizes and increased creaming stability of fish oil-loaded emulsions compared with unmodified gelatins. All these results suggested TG modification was an efficient molecular modification method for gelatins. Moreover, TG-modified aquatic gelatin could be potential mammalian gelatin replacer. This work could provide useful information to understand the relationship among animal sources, tissue sources, extraction methods, amino acid compositions, molecular modification, molecular structure, physicochemical properties, functional properties, and emulsification stability of gelatins.

Effect of carbon numbers and structures of monosaccharides on the glycosylation and emulsion stabilization ability of gelatin

Herein, the effect of saccharide glycosylation by nine monosaccharides on bovine bone gelatin for the stabilization of fish oil-loaded emulsions was explored. The gelatin modification was analyzed and then the emulsifying properties of monosaccharide-modified gelatins were analyzed at pH 9.0 and 3.0. The results demonstrated that glycosylated gelatin structure, droplet stability, creaming stability, and liquid-gel transition time were dependent on monosaccharide carbon numbers, monosaccharide structures, and solution pH. Glycosylation modification of gelatins did not obviously change the emulsion droplet stability at pH 9.0, whereas it increased the emulsion droplet stability at pH 3.0. Glycosylation modification of gelatins did not obviously change the emulsion creaming index values (5.1%–8.4% at pH 9.0 and 25.8%–33.1% at pH 3.0). Three-carbon and four-carbon monosaccharides glycosylation significantly increased emulsion liquid-gel transition times. This work provided useful information to understand the effects of carbon numbers and structures of monosaccharides on the protein modification.

Self-assembled hydrolyzed gelatin nanoparticles from silver carp spine bones for Pickering emulsion stabilization

In this work, enzymatic hydrolysis modification was combined with silver carp spine bone gelatin extraction process to obtain pepsin enzyme hydrolyzed gelatins (PEHGs) for emulsion development. Using pepsins at ratios of 6–24 U/g of silver carp vertebrae, PEHGs were obtained with molecular weights of mainly <5 KDa and the production yields were 12.6%–13.3%. The obtained PEHGs at different pepsin/vertebrae ratios showed similar secondary structure percentages. They could self-assembled into pH-stable nanoparticles. PEHGs had higher fat-binding capacity values (16.2–21.5 g of oil/g of PEHG) and higher emulsion stabilization ability (creaming index values < 11% after 28-day storage at 4 °C) than silver carp scale gelatins, bovine bone gelatin, cold-water CFG and tilapia skin gelatins. With the decrease of pepsin/vertebrae ratios in the PEHG preparation process, the nanoparticle numbers and sizes increased, the turbidities of PEHG solutions increased, the gel strengths (164–314 g) of PEHG gels increased, the initial droplet sizes of Pickering emulsions decreased, and creaming stability of Pickering emulsions increased. This work provided useful information to analyze the effect of enzymatic hydrolysis modification on the structural, functional, and emulsifying properties of a protein. It also provided an efficient way to prepare protein self-assembly nanoparticles from animal tissues.

The Anti-Inflammatory Effect of Bovine Bone-Gelatin-Derived Peptides in LPS-Induced RAW264.7 Macrophages Cells and Dextran Sulfate Sodium-Induced C57BL/6 Mice.

The bioactive peptides hydrolyzed from bone collagen have been found to possess health-promoting effects by regulating chronic diseases such as arthritis and hypertension. In the current study, the anti-inflammatory effect of bovine bone gelatin peptides (GP) was evaluated in 264.7 macrophages cells and followed by animal trials to investigate their interference on inflammatory cytokines and gut microbiota compositions in dextran sodium sulfate (DSS)-induced C57BL/6 mice. The GP was demonstrated to alleviate the extra secretion of interleukin-6 (IL-6), nitric oxide (NO) and tumor necrosis factor-α(TNF-α) in lipopolysaccharide (LPS)-induced RAW264.7 cells. In DSS-induced colitis mice, the gavage of GP was demonstrated to ameliorate the IBD symptoms of weight loss, hematochezia and inflammatory infiltration in intestinal tissues. In serum, the proinflammatory cytokines (TNF-α,IL-6, MCP-1, IL-1β) were suppressed along with the decreasing effect on toll-like receptor 4 and cyclooxygenase-2 by GP treatment. In the analysis of gut microbiota, the GP was checked to modulate the abundance of Akkermansia, Parasutterella, Peptococcus, Bifidobacterium and Saccharibacteria. The above results imply that GP could attenuate DSS-induced colitis by suppressing the inflammatory cytokines and regulating the gut microbiota.

Hyaluronic acid-rich burger separator edible disc prepared from slaughterhouse waste.

In this study, the edible films from chicken feet (CF), ovine muscle fascia (MF), and bovine bone gelatin (Gel) were prepared and their characteristics were analyzed, and we also evaluated the sensory quality of raw and cooked hamburgers using the edible films. The quantities of the CF and MF hyaluronic acid were evaluated using colorimetry and spectrophotometry. The CF, MF, and Gel films were prepared by solvent casting method. Results indicated that the concentration of hyaluronic acid in CF (124.11ppm) was greater than MF (101.11ppm). The antioxidative property of the CF film (18.47%) was greater than the Gel (1.88%) and MF (Undetectable) film. The CF film was more resistant to water vapor permeability (2.75×10-9g/m.s.pa) than the MF (1.57×10-8g/m.s.pa) and Gel (1.5×10-7g/m.s.pa) films. The Gel film had more appropriate mechanical properties than CF and MF films. The films kept burgers patties independent from one another and prevented them from sticking and freezing together. MF and CF films were able to promote the organoleptic properties of raw and cooked hamburgers in taste and texture.

Anhydride structures affect the acylation modification and emulsion stabilization ability of mammalian and fish gelatins

In this work, ring-like anhydrides (C4, C5, and C6) with different sizes and succinic anhydrides (C4, C10, C12, C14, and C16) with different side chain lengths were used to modify bovine bone gelatin (BBG) and cold-water fish skin gelatin (CFG), and the effect of acylated gelatins on fish oil-loaded emulsions stability was explored. The results showed that the degree of N-acylation decreased with increased ring sizes or side chain lengths, and the surface hydrophobicity of acylated gelatins increased with increased anhydride carbon numbers. Acylated CFGs had higher droplet stability and lower liquid-gel transition time than acylated BBGs. Only BBG-C12 had a slight increase on the creaming stability among these acylated gelatins. These results demonstrated that the gelatins could be modified by all the anhydrides and their emulsion stabilization ability was dependent on the gelatin type and anhydride structure. The results could be beneficial for protein-based emulsifier development and application.

The Potency of Bovine Bone Gelatin as Antihypertensive Agent: A Review

This review was purposed to understand the effectiveness of bovine bone gelatin as an antihypertensive agent. This review concerning the effectiveness of bovine bone gelatin as an antihypertensive agent. Hypertension, also called as a silent disease, has become the main cause of coronary heart disease and stroke that contributes to the malfunction of human organs. Changes of lifestyle alongside with science enhancement, provides new inventions regarding methods of hypertension therapy by minimizing the use of synthetic drugs. Collagen tissue of bovine bone gelatin is known to contain angiotensin converting enzyme (ACE) inhibitor, an active peptide that plays a role in lowering blood pressure supporting with the large amount of Gly (27%), Pro (17.6%), and Hyp (14.4%) and repeating pattern of Gly-X-Y. A study was carried out in vivo using injected spontaneously hypertensive rats (SHR) with 30 mg/kg and was able to reduce blood pressure by 15 mmHg. Antihypertensive test with SHR tail-cuff at 30 mg/kg bovine gelatin hydrolysate RGL-(Hyp)-GL and RGM-(Hyp)-GF were 31.3 mmHg and 38.6 mmHg respectively. A study conducted using bovine and porcine gelatin with 30–50 kDa (permeate P1) and 1–2 kDa (permeate P3) was able to reduce blood pressure by 22 mmHg and 21.33 mmHg. In addition, it is still possible conducting research to find out other peptides of bovine bone gelatin that can be used as a future alternative antihypertensive agent.