Functional Properties of Bovine Bone Gelatin and Impact on
Physicochemical, Microbiological and Organoleptic Quality of Set
Yogurt

Arioui, Fatiha; Saada, Djamel Ait; Cheriguene, Abderrahim

doi:10.3923/biotech.2018.1.11

Cited by 12 publications

(13 citation statements)

References 42 publications

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“…The FC increased with the concentrations of the gelatine and its hydrolysate. The FC values of the gelatine and its hydrolysate were lower than that of Nile tilapia bone (Tinrat & Sila-Asna, 2017) and bovine bone (Arioui, 2018).…”

Section: Foaming Propertiesmentioning

confidence: 70%

Functional properties and antioxidant activity of gelatine and hydrolysate from deer antler base

Liu

Xia

Mei

et al. 2020

Food Science & Nutrition

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Gelatine was extracted from deer antler base by the hot water method and hydrolyzed with trypsin. A comparison of the properties of gelatine before and after enzymatic hydrolysis showed a decline in the surface hydrophobicity, enhanced thermal stability, broadening of the particle size distribution, a zeta potential shift to a lower pH, reduced foaming and emulsifying properties, and enhanced antioxidant activity. Hydrolysis increased the gelatine antioxidant activity in DPPH and FRAP assays. These results indicate that the functional properties of deer antler base gelatine may be affected by trypsin modification.

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Section: Foaming Propertiesmentioning

confidence: 70%

Functional properties and antioxidant activity of gelatine and hydrolysate from deer antler base

Liu

Xia

Mei

et al. 2020

Food Science & Nutrition

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“…Peptides with smaller MWs can reach the air-water surface phase, resulting in better FE [73]. FE and FS were different from extracted bovine bone gelatin with acetic acid at 150.66% and 114.66%, respectively [74].…”

Section: Discussionmentioning

confidence: 96%

Characterization and functional properties of gelatin from goat bone through alcalase and neutrase enzymatic extraction

et al. 2021

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Background and Aim: Gelatin is a dissolved protein that results from partial extraction of collagen, commonly from pig and bovine skin. There was no study on gelatin production from Kacang goat bones through enzymatic extraction. This study aimed to evaluate the chemical, physical, and functional properties of gelatin from bones of Kacang goat using alcalase and neutrase enzymes. Materials and Methods: Male Kacang goat bones aged 6-12 months and two commercial enzymes (alcalase and neutrase) were used for this study. Descriptive analysis and completely randomized design (one-way analysis of variance) were used to analyze the chemical, physical, and functional properties of gelatin. Kacang goat bone was extracted with four concentrations of alcalase and neutrase enzymes, namely, 0 U/g (AG-0 and NG-0), 0.02 U/g (AG-1 and NG-1), 0.04 U/g (AG-2 and NG-2), and 0.06 U/g (AG-3 and NG-3) with five replications. Results: The highest yield of gelatin extraction with alcalase obtained on AG-3 was 9.78%, and that with neutrase on NG-3 was 6.35%. The moisture content of alcalase gelatin was 9.39-9.94%, and that of neutrase gelatin was 9.15-9.24%. The ash and fat content of gelatin with alcalase was lower than that without enzyme treatment with higher protein content. The lowest fat content was noted in AG-1 (0.50%), with protein that was not different for all enzyme concentrations (69.65-70.21%). Gelatin with neutrase had lower ash content than that without neutrase (1.61-1.90%), with the highest protein content in NG-3 (70.89%). The pH of gelatin with alcalase and neutrase was 6.19-6.92 lower than that without enzymes. Melting points, gel strength, and water holding capacity (WHC) of gelatin with the highest alcalase levels on AG-1 and AG-2 ranged from 28.33 to 28.47°C, 67.41 to 68.14 g bloom, and 324.00 to 334.67%, respectively, with viscosity that did not differ, while the highest foam expansion (FE) and foam stability (FS) were noted in AG-1, which were 71.67% and 52.67%, respectively. The highest oil holding capacity (OHC) was found in AG-2 (283%). FS and OHC of gelatins with the highest neutrase levels in NG-2 were 30.00% and 265.33%, respectively, while gel strength, viscosity, FE, and WHC of gelatins with the highest neutrase levels did not differ with those without enzymes at all enzyme concentrations. B chain was degraded in all gelatins, and high-intensity a-chains in gelatin with alcalase and peptide fraction were formed in gelatin with neutrase. Extraction with enzymes showed loss of the triple helix as demonstrated by Fourier transform infrared spectroscopy. Conclusion: Based on the obtained results, the Kacang goat bone was the potential raw source for gelatin production. Enzymatic extraction can increase the quality of gelatin, especially the alcalase (0.02-0.04 U/g bone) method. This can be used to achieve the preferable quality of gelatin with a higher yield.

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“…Though Liu et al, successfully prepared gelatin nanofibers from HMWFG using their custom-built airbrush device, they were unsuccessful in fabricating nanofibers using gelatin of mammalian origin . It is important to note that commercially available gelatin is mainly from skins and skeletons of bovine and porcine origin . Hence, there is a need to find out suitable airbrushing parameters to prepare gelatin nanofibers of animal origin by airbrushing method for various biomedical applications.…”

Section: Introductionmentioning

confidence: 99%

“…22 It is important to note that commercially available gelatin is mainly from skins and skeletons of bovine and porcine origin. 23 Hence, there is a need to find out suitable airbrushing parameters to prepare gelatin nanofibers of animal origin by airbrushing method for various biomedical applications.…”

Section: ■ Introductionmentioning

confidence: 99%

Fabrication, Characterization, and Biological Evaluation of Airbrushed Gelatin Nanofibers

Singh

Khan

Basu

et al. 2019

ACS Appl. Bio Mater.

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Gelatin nanofibers have gained significant attention for different biomedical applications, as they provide a suitable environment for cell attachment, growth, and proliferation compared to the other biopolymers and synthetic polymers. Airbrushing/solution-blow-spinning could overcome the limitation of the conventional electrospinning method of nanofiber preparation. The present study reports the fabrication of nano/microfibers from commercially available low-molecular-weight gelatin of animal origin as a first-time study. The effect of various airbrushing parameters, namely, the concentration of gelatin solution, air pressure, and polymer solution flow rate on the fiber quality, morphology, and diameters, was studied. Finally, the biological evaluation of the airbrushed gelatin nanofibers was performed using human bone marrow-derived mesenchymal stem cells (hBMSCs). Gelatin nanofibers exhibit excellent biocompatibility and support the growth of hBMSCs similar to electrospun gelatin nanofibers. Our airbrushing technique is an easy, low-cost, and scalable method to fabricate the gelatin nanofibers for different biomedical applications such as tissue engineering, wound healing, and substrate for delivery of bioactive molecules.

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Functional Properties of Bovine Bone Gelatin and Impact on Physicochemical, Microbiological and Organoleptic Quality of Set Yogurt

Cited by 12 publications

References 42 publications

Functional properties and antioxidant activity of gelatine and hydrolysate from deer antler base

Functional properties and antioxidant activity of gelatine and hydrolysate from deer antler base

Characterization and functional properties of gelatin from goat bone through alcalase and neutrase enzymatic extraction

Fabrication, Characterization, and Biological Evaluation of Airbrushed Gelatin Nanofibers

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