Complex coacervation of low methoxy pectin with three types of gelatins for the encapsulation of fish oil.

Herein, the complex coacervation of low methoxy pectin (LMP) with three types of gelatins was explored to encapsulate fish oil. The fish oil@gelatin-LMP complex coacervates with good precipitation separation could be obtained at low gelatin concentrations (Fish gelatin, FG: 10-80 mg/mL; porcine skin gelatin, PSG: 10-40 mg/mL; bovine skin gelatin, BSG: 10-80 mg/mL), high gelatin: fish oil mass ratios (4:1-1:1), appropriate gelatin: LMP mass ratios (3:1-12:1 for FG and PSG, 6:1 for BSG), and appropriate pH (FG: 4.90-5.50; PSG: 4.80-5.40; BSG: 4.10-4.50). FG induced similar loading ability, lower encapsulation ability, and comparable peroxide values to the mammalian gelatins. FG induced higher or similar free fatty acid released percentages to mammalian gelatins in the in vitro gastrointestinal model at low gelatin concentrations (10-40 mg/mL). These results provided useful information to understand the protein-polysaccharide complex coacervation to encapsulate oil-based bioactive substances.

Effect of Adding Bovine Skin Gelatin Hydrolysates on Antioxidant Properties, Texture, and Color in Chicken Meat Processing.

(1) Background: Phosphates are used in the food industry to improve water retention and product quality. However, when consumed in excess, they can be harmful to health. Instead, bovine skin gelatin hydrolysates present health benefits such as being a rejuvenating agent, stimulating collagen production, and improving food quality, in addition to being a source of protein. The effect of the addition of bovine skin gelatin hydrolysates on the texture and color of thermally processed chicken meat (boiled type) and antioxidant activity was evaluated. (2) Methods: Hydrolysates were prepared with subtilisin with the degree of hydrolysis being 6.57 and 13.14%, which were obtained from our previous study. (3) Results: The hydrolysates improved the firmness of the meat matrix compared to the control. Additionally, the hydrolysate with a 13.14% degree of hydrolysis reached the same firmness (p > 0.05) as the commercial ingredient sodium tripolyphosphate at its maximum limit allowed in the food industry when it was applied at 5% (w/w meat) in the meat matrix, improving firmness over the control by 63%. Furthermore, both hydrolysates reached a similar color difference to sodium tripolyphosphate at its maximum allowed limit when applied at a concentration of 2% (w/w meat). Additionally, it was found that these hydrolysates obtained the same antioxidant activity as sodium tripolyphosphate, capturing free radicals at 10%. (4) Conclusion: The findings of this study suggest that bovine skin gelatin hydrolysates can be applied as an ingredient with functional properties, being an alternative to phosphates to improve the quality of meat products.

Thermo-Tunable Pores and Antibiotic Gating Properties of Bovine Skin Gelatin Gels Prepared with Poly(n-isopropylacrylamide) Network.

Polystyrene nanospheres (PNs) were embedded in bovine skin gelatin gels with a poly(N-isopropylacrylamide) (PNIPAAm) network, which were denoted as NGHHs, to generate thermoresponsive behavior. When 265 nm PNs were exploited to generate the pores, bovine skin gelatin extended to completely occupy the pores left by PNs below the lower critical solution temperature (LCST), forming a pore-less structure. Contrarily, above the LCST, the collapse of hydrogen bonding between bovine skin gelatin and PNIPAAm occurred, resulting in pores in the NGHH. The behavior of pore closing and opening below and above the LCST, respectively, indicates the excellent drug gating efficiency. Amoxicillin (AMX) was loaded into the NGHHs as smart antibiotic gating due to the pore closing and opening behavior. Accordingly, E. coli. and S. aureus were exploited to test the bacteria inhibition ratio (BIR) of the AMX-loaded NGHHs. BIRs of NGHH without pores were 48% to 46.7% at 25 and 37 °C, respectively, for E. coli during 12 h of incubation time. The BIRs of nanoporous NGHH could be enhanced from 61.5% to 90.4% providing a smart antibiotic gate of bovine skin gelatin gels against inflammation from infection or injury inflammation.

Distinguishing tissue origin of bovine gelatin in processed products using LC/MS technique in combination with chemometrics tools.

Gelatin, as a by-product of the meat industry, is extracted from bone and skin of mainly bovine and porcine origins. It is used widely in the food, drug, and cosmetic industries. Authenticity testing methods can be used to confirm whether labelled ingredients are present in the product. Generally, studies on gelatin are concerned mainly with determining species, but detecting tissue origin is also important from religious, health, and commercial perspectives. In the present study, for the first time, liquid chromatography/mass spectrometry (HPLC/MS) was used to differentiate bovine bone gelatin from gelatin derived from bovine skin. Tryptic-digested gelatins were measured using HPLC/MS and, subsequently, two powerful chemometrics approaches (i.e., PCA and PLS-DA) were used to classify samples as either skin or bone gelatins. Origin of bovine gelatins in different test samples were predicted accurately using this method. The results showed both the stability and reliability of the proposed procedure.