Gelatin Extraction Research Articles

EFFECTS OF USING HYDROXIAPATITE-GELATIN GEL AND ROSELLA EXTRACT TO PREVENT RELAPSE IN ORTHODONTIC TREATMENT

To correct malocclusion and malposition in dentistry using orthodontic treatment. Teeth that have moved through the bone with orthodontic devices tend to return to their original position or what is usually called relapse. Relapse is when the teeth return to their original position before orthodontic treatment was carried out. Relapse prevention can be achieved using mechanical devices but there are still some limitations. The use of scaffolds can be a solution in preventing tooth relapse because scaffolds can support cells to grow and develop into new bone in the damaged area. The scaffold components are hydroxyapatite, gelatin, and rosella flower extract which contains flavonoids to inhibit bone resorption. To find out whether these components are toxic or not before they are applied to the human body, a cytotoxicity test is carried out, which is a laboratory study. This research was carried out by incubating the hydroxyapatite scaffold, gelatin and rosella flower extract with osteoblast cells for 24 hours to see whether the rosella extract was toxic to osteoblast cells. Conclusion: This toxicity test shows that rosella flower extract as an ingredient in making scaffolds is not toxic to osteoblast cells.

Gelatin Gel from By-products of Sand Jellyfish (Rhopilema hispidum): Physicochemical and Biochemical Characterization

Salted sand-type jellyfish by-products are abundant in collagen, which may be processed into gelatin to decrease food waste. From the production standpoint, various factors affect gel qualities, including raw material used, pretreatment methods, and extraction times. So far, gelatin extracted from desalted sand-type jellyfish by-products (D-SJB) must be adequately characterized. Therefore, this research aimed to characterize gelatin from D-SJB using different pretreatment methods and extraction times. D-SJB was treated with 0.2 M hydrochloric acid (acid method) and extracted for 24 h at 60 °C (SA24), the optimal gelatin extraction condition with the highest gel qualities, while the jellyfish gelatin obtained after D-SJB was treated with pepsin and extracted for 48 h had the lowest gel qualities. The viscosity, gel strength, gelling temperature, and melting temperatures of SA24 were 20.80 cP, 352.22 g, 11.97 °C, and 22.70 °C, respectively. All jellyfish gelatin’s gelling and melting temperatures ranged from 6.13−11.97 °C and 15.85−22.70 °C, exhibiting a cold set gel and unstable gels at room temperature. The different pretreatment methods and extraction times during the jellyfish gelatin production resulted in the conversion of amides A, B, I, II, and III, especially the wavenumber of the amide I increased after pepsin pretreatment and increased with longer extraction time. Twenty-one collagen subtypes in bovine, fish, and jellyfish gelatin were analyzed using LC-MS/MS. The collagen alpha-2(I) chain, a key gelatin component, was identified in all gelatins. The research novelty showed the profound characterization results of gelatin gel produced from D-SJB. However, further experiments will be needed for pilot-scale production to be used in food and non-food applications.

Extraction and characterisation of gelatine from yellowfin tuna skin pretreated with a eutectic solvent

The accumulation and management of waste generated during the processing of seafood products is one of the major current challenges in the fishery industry. Among these residues, fish skin stands out for its high collagen content, from which high-quality gelatine can be obtained. However, conventional methods for gelatine extraction are time-consuming and complex processes that involve the use of strong acidic and alkaline solutions, leading to serious environmental concerns. This research studied the use of a eutectic solvent, formed by two safe and environmentally friendly compounds such as sodium acetate trihydrate and urea, to pretreat the skin of yellowfin tuna before the extraction of gelatine. Two different times of pretreatment were tested, and the subsequent extraction was carried out in warm water, resulting in much higher yields of gelatine (0.3 g/g wet fish skin) than previous studies. Additionally, using FT-IR analysis and amino acid profiling, it was observed that the pretreatment time did not significantly affect the structure or composition of the gelatine. However, some variation was found in its molecular weight distribution and therefore in its rheological properties: with an increase in the pretreatment time, both the molecular weight and the storage modulus of the gel also increased, as well as the gelation and melting temperatures. This contribution offers a simplified process that reduces environmental impact and provides the opportunity to tailor the final product.

Extraction and characterization of new biocompatible gelatin from camel slaughter by-products: biochemical, sensory, interfacial, and textural properties

Extraction and characterization of new biocompatible gelatin from camel slaughter by-products: biochemical, sensory, interfacial, and textural properties

Effects of the extraction temperatures on the protein contents, gelatin purities, physicochemical properties, and functional properties of tilapia scale gelatins

Herein, the effects of the extraction temperatures (45, 55, 65, 75, and 85 °C) on the protein contents, gelatin purities, physicochemical properties, and functional properties of tilapia scale gelatins were studied. Among these temperatures, 65 °C was the best extraction temperature to obtain good production yield (16.0 % ± 0.3 %), good protein contents (excellent total amino acid composition of 94.20 ± 0.76 g/100 g of gelatin, the highest hydrophobic amino acids percentage of 32.68 ± 0.24 g/100 g of gelatin), appropriate ATR-FTIR spectra peaks (Amides A, B, I, II, and III), high β-sheet percentage (38.2 % ± 1.3 %), the highest purity of the gelatin structures (280, 140, and 125 kDa), the lowest nanoparticle sizes in atomic force microscopy results, the highest water-holding capacity (25.3 % ± 0.9 %), the highest fat-binding capacity (16.9 % ± 0.1 %), high foaming properties (foaming capacity of 151.7 % ± 7.6 % and foaming stability of 145.8 % ± 6.3 %), the lowest interfacial tension (2.1 ± 0.2 mN/m), the lowest emulsifying activity index (16.5 % ± 0.9 %), the highest emulsifying stability index (88.9 % ± 5.1 %), highest emulsion viscosity (1462 ± 17 mPa·s at the rotary speed of 6 rpm), the lowest initial droplet sizes, and lowest emulsion creaming index (6.9 % ± 0.7 %). This work provided a useful guide to choosing extraction temperature for gelatin extraction and a useful theory on the relationship between compositions and properties of a protein sample.

Effects of Acid Pre-Treatment on Removal of Organic and Inorganic Substances from Black Tilapia Bones and Scales

Fish bones and scales are good sources of gelatin. However, high mineral content in bones and scales often lead to low quality gelatin with high percentage of ash. Therefore, pre-treatment with acid prior to gelatin extraction is necessary. Black tilapia (Oreochromis niloticus) bones and scales were subjected to Hydrochloric (HCl) acid of 0.6 M to 1.4 M for 0 to 32 hr. The suitable pre-treatment conditions were determined using percentage of ash removed and loss of protein from the samples. Results obtained indicate, 99.86 % and 99.84 % of ash can be removed from bones and scales, with 1.4 M HCl (32 hr) and 1.0 M HCl (10 hr), respectively. Further analysis with UV-Vis revealed that, excessive protein breakdown starts to occur at 1.0 M (32 hr) and 0.6 M (12 hr), in bones and scales, respectively. The data suggest using pre-treatment conditions lower than the above to avoid protein loss which may lead to low gelatin yield.

Physicochemical and functional properties of buffalo (Bubalus bubalis) bone gelatin extracted using acid pre-treatment

This study explored the effects of pre-treatment conditions using hydrochloric acid and citric acid at concentrations of 0.025 M and 0.05 M, on the properties and extractability of gelatin sourced from buffalo bone. The highest yield (6.36 %) and hydroxyproline content (26.98 g/100 g) were obtained from gelatin extracted using 0.025 M HCl pre-treatment (H-1). In comparison, pre-treatment with 0.05 M citric acid (C-2) resulted in the lowest yield (3.79 %) with hydroxyproline content of 12.49 g/100 g. Buffalo bone gelatin had considerably lower moisture content ranging from 7.54 % to 11.92 % than standard bovine gelatin (SBG) (10.91 %) and a pH range of 5.31 to 5.44, indicating it is Type A gelatin. The gelatin that subjected to the pre-treatment by 0.025 M citric acid (C-1) illustrated the highest values for emulsion activity index (EAI), emulsion stability index (ESI), foaming expansion (FE), foaming stability (FS), water holding capacity (WHC), and fat binding capacity (FBC). Fourier Transform Infrared Spectroscopy (FTIR) results indicated a similar secondary structure to SBG explained by the presence of Amide A, B, I, II and III components. Apparent peptides at the α and β regions were observed in the buffalo bone gelatin. Buffalo bone gelatin shows potential as an alternative source of halal gelatin manufacturing.

Comparative analysis of red skin Tilapia and bovine gelatins as halal alternatives in food industry

Gelatin plays a vital role in the food industry, serving as a thickening agent, emulsifier, wetting agent, and stabiliser. However, conventional sources like mammalian gelatin pose health and societal issues, while poultry gelatin can present risks related to avian flu. Our work was motivated by recent studies focusing on alternative gelatin sources, which prompted further investigation. Our study aimed to extract gelatin from red-skin Tilapia and bovine sources. Both types of gelatin underwent pre-treatment using 0.2 M sodium hydroxide (NaOH) and 0.05 M acetic acid (CH3COOH) at 27ºC, followed by water extraction at 60°C for 3 hours. Fourier-transform infrared (FTIR) analysis confirmed that the extracted gelatins exhibited peaks similar to commercial gelatin. The extracted fish gelatin (EFG) demonstrated superior gel strength compared to commercial fish gelatin (CFG), whereas commercial bovine gelatin (CBG) exhibited superior gel strength than extracted bovine gelatin (EBG). The protein content of EFG and EBG was comparable, but the fat content was significantly higher in EFG. The foaming capacity was also evaluated, with EFG showing greater capacity than EBG. Our work demonstrates excellent potential of alternative gelatin for usage in various applications and creates new opportunities for the food sector, particularly for halal food production.

Extraction and physicochemical characterization of native and broiler chicken feet gelatin.

Poultry processing generates a large amount of industrial waste, which is rich in collagen content. This waste can be utilized for the extraction of valuable components such as gelatin, which can be used as an alternative to mammalian gelatin (porcine and bovine). Gelatins were analyzed for their yield, proximate analysis, pH, color, viscosity, bloom strength, and texture profile analysis. The yield of broiler chicken feet gelatin (BCFG) was slightly higher (7.93%) as compared to native chicken feet gelatin (NCFG) (7.06%). The protein content was 85.92% and 82.53% for BCFG and NCFG. Both gelatin had moisture content in the standard range (< 15) as given by Gelatin Manufacturers of Europe (GME). Both gelatins showed higher bloom strength (326 g for NCFG and 203 g for BCFG) at 6.67% gelatin concentration, classified as high bloom. Fourier-transform infrared (FTIR) analysis showed amide I, amide A, amide B at 1636 cm-1, 3302 cm-1, 2945 cm-1 for NCFG and 1738 cm-1, 3292 cm-1, 2920 cm-1 for BCFG. At 6.67% gelatin concentration, hardness and cohesiveness values were also higher than commercial gelatin previously studied. The pH values for NCFG were 5.43 and BCFG was 5.31. Both NCFG and BCFG viscosities (4.43 and 3.85 cP) were in the optimum range of commercial gelatins (2-7 cP). Hence, the present study concluded that both NCFG and BCFG have a huge potential to replace commercial mammalian gelatins (porcine and bovine) in the food industries. However further studies should be done to optimize the extraction process. © 2024 Society of Chemical Industry.

Rosettibacter primus gen. nov., sp. nov., and Rosettibacter firmus sp. nov., facultatively anaerobic moderately thermophilic bacteria of the class Ignavibacteria from hot springs of North Ossetia

A novel facultatively anaerobic moderately thermophilic bacteria, strains 4137-MeT and 4148-MeT, were isolated from hot springs of Karmadon and Ursdon, respectively (North Ossetia, Russian Federation). Gram-negative, motile rods were present singly, in pairs, rosettes, and aggregates, or formed biofilms. Both strains grew optimally at 50–55 °C, pH 7.0 and did not require sodium chloride or yeast extract for growth. They were chemoorganoheterotrophs, growing on mono-, di- and polysaccharides (cellulose, starch, xylan, lichenan, galactan, xyloglucan, mannan, xanthan gum, guar gum) as well as proteinaceous substrates (gelatin, peptone, beef and yeast extract). Growth under anaerobic conditions was observed in presence and absence of external electron acceptors. Sulfur, thiosulfate, arsenate, Fe-citrate, and ferrihydrite were reduced with acetate, starch, or yeast extract as electron donors. The respiratory quinone was MK-7. Major cellular fatty acids of both strains were iso-C15:0, anteiso-C17:0, C15:0, iso-C16:0 and additionally iso-C17:0 for strain 4137-MeT. The size of the genome and genomic DNA G + C content of strain 4137-MeT were 3.24 Mb. and 29.9 %, respectively; for strain 4148-MeT – 3.33 Mb and 30.7 %. According to the 16S rRNA gene sequence and conserved protein sequences phylogenies, strains 4137-MeT and 4148-MeT represented a distinct lineage of the family Melioribacteraceae within the class Ignavibacteria. Based on phylogenetic analysis and phenotypic features, the novel isolates were assigned to a novel genus, for which the name Rosettibacter gen. nov. is proposed. Strain 4148-MeT represents its type species Rosettibacter primus sp. nov., while strain 4137-MeT represents a new species Rosettibacter firmus sp. nov.

Valorization of Yellowfin Tuna Tails: From Proteolytic Enzyme Production to Gelatin and Antioxidant Hydrolysate Extraction.

This study investigates the valorization potential of yellowfin tuna (Thunnus albacares) tails to produce high-value commercial products. Firstly, the tuna tails were placed in a perforated stainless-steel cylinder, and hydraulic pressure was applied to separate the skin from the muscle in the tails. The extracted muscle was then utilized as a nitrogen source for the growth of the proteolytic enzyme producer Bacillus subtilis, while the skins were employed for gelatin extraction. The proteases from B. subtilis were partially purified and used to produce antioxidant peptides from the obtained gelatin. The gelatin formed a gel upon cooling, with gelling and melting temperatures of 16 °C and 22 °C, respectively, and a Bloom strength of approximately 160. Response Surface Methodology (RSM) was employed to determine the optimal hydrolysis conditions to achieve the highest antioxidant activity (35.96% measured as DPPH radical scavenging activity), which were 50 °C and 6.5 IU of enzyme. The findings emphasize the importance of an integrated approach to maximize the value of tuna by-products, promoting sustainability within the framework of a circular bioeconomy. Overall, these results contribute to the efficient utilization of tuna by-products, waste reduction, and enhanced economic viability of the tuna industry.

Development of Biodegradable Bioplastics with Sericin and Gelatin from Silk Cocoons and Fish Waste.

The bioplastics sector promotes environmentally friendly means of cutting down on the usage of fossil fuels, plastic waste, and environmental pollution. Plastic contamination has detrimental effects on both ecological systems and the global food supply. The approach we present here to resolve this issue involves the integration of sericin and gelatin, obtained from cocoon and fish waste, respectively, with nano-reinforced cellulose crystals, to develop a biodegradable and compostable plastic material. The use of cocoon and fish wastes for the extraction of sericin and gelatin presents an environmentally beneficial approach since it contributes to waste reduction. The sericin level found in silk cocoon waste was determined to be 28.08%, and the gelatin amount in fish waste was measured to be 58.25%. The inclusion of sericin and gelatin in bioplastics was accompanied by the incorporation of glycerol, vinegar, starch, sodium hydroxide, and other coloring agents. Fourier transform infrared (FTIR) examination of bioplastics revealed the presence of functional groups that corresponded to the sericin and gelatin components. The tensile strength of the bioplastic material was measured to be 27.64 MPa/psi, while its thickness varied between 0.072 and 0.316 mm. The results of burial experiments indicated that the bioplastic material had a degradation rate of 85% after 14 days. The invention exhibits potential as a viable alternative for packaging, containment, and disposable plastic materials. The use of this sustainable approach is recommended for the extraction of sericin and gelatin from silk cocoons and fish waste, with the intention of using them as raw materials for bioplastic production.

Gelatin and Collagen from Sheepskin.

Abattoirs dispose of sheepskins as solid waste due to low price and poor demand for sheepskin leather. In principle, as an alternative to being disposed of in landfill, sheepskins can serve as a source of the protein collagen or the hydrolysis product, gelatin. In this research, sheepskins collected from abattoirs were used as a source of collagen. Three extraction methods were compared: acid extraction, acid with enzymes, and alkali extraction. The extracted material was characterized using scanning electron microscopy (SEM) and Fourier-transform infrared spectroscopy (FTIR), small angle X-ray scattering (SAXS), and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The collagen and gelatin extraction yield ranged from 3.1% to 4.8% with the product purity determined by hydroxyproline, ranging from 7.8% for the alkali process to 59% and 68% for the acid and acid-enzyme processes. SDS PAGE showed that the acid process produced fragments with molecular weights in the range 100 to >250 kDa, while acid-enzyme resulted in smaller fragments, below 30 kDa. The FTIR region of the amide I band at 1800-1550 cm-1, which was used as an indicator of the collagen and gelatin content, showed that the gelatin dominated in the acid extracts, and the alkaline extract contained a large portion of keratin. SAXS was found to be a sensitive method for showing the presence of intact collagen fibrils in materials from all of the extraction methods, albeit at low concentrations. Herein, sheepskin is shown to be a useful source for collagen-gelatin material of varying molecular weights.

Sequential extraction and characterization of gelatin from turkey (Meleagris gallopavo) feet

Sequential extraction and characterization of gelatin from turkey (Meleagris gallopavo) feet

Influence of Gelatin and Propolis Extract on Honey Gummy Jelly Properties: Optimization Using D-Optimal Mixture Design.

Gelatin is commonly used as a gelling agent in gummy candy. Honey and bee products are valuable and rich sources of biologically active substances. In this study, the influence of gelatin and propolis extract on honey gummy jelly (HGJ) properties was investigated. Honey (28-32%), xylitol (13-17%), and gelatin (6-10%) were utilized to develop HGJ products by mixture design methodology. Subsequently, the optimized formulation of HGJ was fortified with 1% and 2% propolis extract to enhance its phytochemicals and antimicrobial activities. The variation in the ingredients significantly affected the physicochemical, textural, and sensory properties of the HGJ. The optimized HGJ formulation consisted of honey (32%), xylitol (14%), and gelatin (7%) and exhibited 13.35 × 103 g.force of hardness, -0.56 × 103 g.sec of adhesiveness, 11.96 × 103 N.mm of gumminess, 0.58 of resilience, and a moderate acceptance score (6.7-7.5). The fortification of HGJ with propolis extract significantly increased its phytochemical properties. Furthermore, the incorporation of propolis extract (2%) into the HGJ was able to significantly inhibit the growth of Gram-positive (Streptococcus mutans and Staphylococcus aureus) and Gram-negative (Escherichia coli) bacteria. The mixture of gelatin, xylitol, honey, and propolis extract can be utilized to develop a healthy gummy product with acceptable physicochemical, textural, and sensory qualities.

Textural, rheological, and structural properties of turkey and chicken gelatins from mechanical deboning residues.

Large amounts of collagen-rich by-products are generated in poultry processing. In particular, gelatin from the by-products of turkey processing is limited. Gelatin extraction from turkey and chicken MDRs (mechanically deboning residue) was the purpose of this study. Both materials were modified at the highest swelling pH for chemical denaturation of collagen and hot water extraction of gelatin was performed at the optimum temperature-time, which was determined to be pH 1.0 and 80°C-6 h, respectively. In these conditions, yields of 9.90% turkey gelatin (TG) and 13.85% chicken gelatin (CG) were produced. They demonstrated similar viscosity, gel strength, and lightness values of 72-73 g, 2.5-2.7 mPas, and 31, respectively. These results are close to those of bovine gelatin (BG). TG with 239.78 g Bloom exhibited higher strength than CG (225.27 g) and BG (220.00 g). The melting and gelation temperatures of CG and BG were 21 and 30°C, respectively, while those of TG were 19 and 28°C. Imino acids (proline + hydroxyproline) of TG (22.82%) were higher than those of CG (20.73%). Fourier transform infrared spectroscopy (FTIR) analysis revealed secondary structure and functional groups of CG and TG similar to those of BG. CG displayed a higher thermal transition temperature than BG, while TG exhibited the highest temperature sensitivity, according to the differential scanning calorimetry (DSC) analysis. In conclusion, TG showed higher potential for effective utilization with higher bloom and imino acids. Overall, turkey and chicken MDRs are a promising and potential alternative source to produce gelatin with comparable properties to bovine gelatin for intended food applications as well as for pharmaceutical and cosmetic fields.

Exploring the Model of Cefazolin Released from Jellyfish Gelatin-Based Hydrogels as Affected by Glutaraldehyde.

Due to its excellent biocompatibility and ease of biodegradation, jellyfish gelatin has gained attention as a hydrogel. However, hydrogel produced from jellyfish gelatin has not yet been sufficiently characterized. Therefore, this research aims to produce a jellyfish gelatin-based hydrogel. The gelatin produced from desalted jellyfish by-products varied with the part of the specimen and extraction time. Hydrogels with gelatin: glutaraldehyde ratios of 10:0.25, 10:0.50, and 10:1.00 (v/v) were characterized, and their cefazolin release ability was determined. The optimal conditions for gelatin extraction and chosen for the development of jellyfish hydrogels (JGel) included the use of the umbrella part of desalted jellyfish by-products extracted for 24 h (WU24), which yielded the highest gel strength (460.02 g), viscosity (24.45 cP), gelling temperature (12.70 °C), and melting temperature (22.48 °C). The quantities of collagen alpha-1(XXVIII) chain A, collagen alpha-1(XXI) chain, and collagen alpha-2(IX) chain in WU24 may influence its gel properties. Increasing the glutaraldehyde content in JGel increased the gel fraction by decreasing the space between the protein chains and gel swelling, as glutaraldehyde binds with lateral amino acid residues and produces a stronger network. At 8 h, more than 80% of the cefazolin in JGel (10:0.25) was released, which was higher than that released from bovine hydrogel (52.81%) and fish hydrogel (54.04%). This research is the first report focused on the production of JGel using glutaraldehyde as a cross-linking agent.

Optimization of cobia fish (Rachycentron canadum) gelatin extraction with response surface methodology

Cobia fish or often called sea cork fish, is a fish that has thick meat which is nutritionally equivalent to salmon meat. Cobia fish is usually sold in the form of fish fillets and the bones becomes solid waste, which has the potential to be a raw material for fish gelatin. Gelatin is a bone and skin collagen hydrolysis product that can be used for food and nonfood industries. The quality of fish gelatin is influenced by the extraction process, such as acid concentration, temperature, and extraction time. This study aims to determine the effect of hydrochloric acid concentration, temperature, extraction time, and the optimal process of making cobia fish bone gelatin using the response surface methodology with the Box Behnken model. The data was processed using Design Expert 11 software. The model suggested by the software was the cubic model. The optimum extraction conditions obtained were using a concentration of 5.53% hydrochloric acid, a temperature of 90oC, and a stirring time of 6.42 mins would produce a yield of 12.38% and gel strength of 229.14 bloom. The verification results by extracting cobia fish gelatin with optimum conditions obtained a yield of 11.22% and gel strength of 227.60 bloom. The proximate analysis of cobia fish gelatin extracted under optimum conditions was found to contain 6.43% water content, 8.27% ash content, 4.65% fat content, 68.47% protein content, and 12.18% carbohydrate by different. Cobia fish gelatin microstructure is in the form of thick strands with a soft sponge.

Utilization of Lumpfish (Cyclopterus lumpus) Skin as a Source for Gelatine Extraction Using Acid Hydrolysis.

Lumpfish (Cyclopterus lumpus) is an underutilized marine resource that is currently only being exploited for roe. Lumpfish skin was pre-treated with alkali (0.1M NaOH) and acid (0.1M HCl) at a skin to chemical ratio of 1:10 for 24 h at 5 °C to remove non-collagenous proteins and minerals. The pre-treated skin was washed, and gelatine was extracted with 0.1M of acetic acid at three different ratios (1:5, 1:10, and 1:15), time (12,18, and 24 h), and temperature combinations (12, 28, and 24 °C). The highest total extraction yield (>40%) was obtained with combinations of extraction ratios of 1:15 and 1:10 with a longer time (24 h) and higher temperature (18-24 °C). The highest gelatine content was obtained with an extraction period of 24 h and ratio of 1:10 (>80%). SDS-PAGE analysis confirmed the presence of type-I collagen. A rheological evaluation indicated melting and gelling temperatures, gel strength, and viscosity properties comparable to existing cold-water gelatine sources.

Improvement of heat-sealing strength of chitosan-based composite films and product costs analysis in the production process

The primary objective of this study was to enhance the heat-sealing strength of composite films made from chitosan and analyze the associated product costs. The approach adopted involved formulating chitosan-based composite films by incorporating gelatin and green seaweed extract. This strategic combination resulted in a notable improvement in heat-sealing strength. The ensuing attributes underwent meticulous examination, encompassing seal strength, FTIR spectroscopy, FE-SEM surface morphology analysis, and DSC thermal properties determination. Data analysis was rigorously conducted using the SPSS program, with outcomes presented as mean values accompanied by standard deviations. Disparities were discerned at a 95% confidence level, ensuring statistical robustness. The findings unveiled that the incorporation of 10% gelatin and 1% green seaweed extract substantially enhanced the seal strength of the chitosan-based composite films. Notably, the introduction of green seaweed extracts disrupted interactions between chitosan's structure and various molecular vibrations. This disruption, coupled with increased ionic interactions and hydrogen bonding, led to improved molecular interdiffusion, ultimately resulting in modified heat sealability. The study identified the optimized conditions as 10% gelatin and 1% green seaweed extract concentrations, which produced the highest seal strength at 19.4 N/m. Further evidence from scanning electron microscopy demonstrated improved interfacial adhesion, attributed to the adjusted surface morphology. The film surface did not contain small scattered particles and presented a smooth phase. This suggests that the chitosan-based composite achieved good interfacial adhesion between the two components in these films. As an essential aspect for practical application, the total production cost of the films was determined to be 606.84 baht. This information renders the data collection from the study valuable for companies seeking to enhance production efficiency and overall profitability.