Gelatin

Vergauwen, Bjorn; Stevens, Paul; Prawitt, Janne; Olijve, Jos; Brouns, Ellis; Babel, Wilfried; Schulz, Dieter; Giesen-Wiese, Monika; Seybold, Uwe; Gareis, Herbert; Dick, Eberhard; Schrieber, Reinhard; Schott, Annelore; Stein, Winfried

doi:10.1002/14356007.a12_307.pub2

Cited by 3 publications

(4 citation statements)

References 32 publications

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“…Moreover, the RH with gelatin showed the second-highest score for sensory properties. According to the study by Vergauwen et al [ 2 ], gelatin can improve sensory properties because it has a strong water-binding ability due to a large number of polar amino acids and does not have a characteristic odor.…”

Section: Resultsmentioning

confidence: 99%

“…Multiple hydrophobicity sites are found in meat proteins, and gelatin has many hydrophobicity areas on its surface [ 11 ]. Amphiphilic behavior, such as foaming and emulsifying capabilities, is influenced by the ratio of hydrophobic to hydrophilic amino acids [ 2 ]. The aggregation of meat proteins was aided by high hydrophobic forces among proteins, while the hydrophobicity of the RH with the addition of gelatin and TGase was reduced [ 30 ].…”

Section: Resultsmentioning

confidence: 99%

“…It has been generally applied to various foods, beverages, and pharmaceuticals. It is utilized in meat products as a gelling and binding agent because it has a high number of polar amino acids, which improves the hydration qualities [ 1 , 2 ].…”

Section: Introductionmentioning

confidence: 99%

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Effect of Pork Skin Gelatin on the Physical Properties of Pork Myofibrillar Protein Gel and Restructured Ham with Microbial Transglutaminase

Lee

Chin²

2022

Gels

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The goal of this study was to determine the qualities of pork myofibrillar protein (MP) gels added with pork gelatin and transglutaminase (TGase), as well as their application to restructured ham (RH). MP mixtures were prepared with various levels of gelatin (0.5, 1.0, and 1.5%. w/w) and TGase. In this study, cooking loss (CL), gel strength, shear stress, and the microstructure of MP with various levels of gelatin were evaluated. After RHs were manufactured with varying levels of gelatin and TGase, the physicochemical and textural properties were measured. The CL of the MP with 1% (w/w) of gelatin was decreased. Regardless of the presence of TGase, increased amounts of gelatin in the MP gels resulted in high shear stress. Shear values were higher in the RH with gelatin treatment than in the other treatments. In addition, the RHs with gelatin alone or combined with TGase had high water-holding capacity. The RH with the combination of gelatin and TGase had higher sensory attributes than the control. Gelatin improved the physical properties of the RHs and is recommended for application in various meat products.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Effect of Pork Skin Gelatin on the Physical Properties of Pork Myofibrillar Protein Gel and Restructured Ham with Microbial Transglutaminase

Lee

Chin²

2022

Gels

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“…in medical research [ 8 , 9 ], food chemistry [ 10 ] and paleoprotein analysis [ 11 – 14 ]. Food products with animal material as an ingredient often contain collagen type 1, either due to its ubiquity and high abundance in (extracts from) animal tissues and/or by the intended addition of gelatin, which is partly hydrolyzed collagen often obtained from skin or bone [ 15 , 16 ]. For religious or lifestyle reasons it may be important for consumers to know whether food products contain animal material and, if so, of which species.…”

Section: Introductionmentioning

confidence: 99%

The quest for a generic bird target to detect the presence of bird in food products and considerations for paleoprotein analysis

Kleinnijenhuis¹,

Holthoon²

2022

PLoS ONE

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It can be important for consumers to know whether food products contain animal material and, if so, of which species. Food products with animal material as an ingredient often contain collagen type 1. LC-MS/MS (Liquid Chromatography–tandem Mass Spectrometry) was applied as technique to generically detect bird. Unlike for example fish, that have experienced longer divergence times, it is still possible to find generic LC-MS targets for avian type 1 collagen. After theoretical target selection using 83 collagen 1α2 bird sequences of 33 orders and construction of a common ancestor sequence of birds, experimental evidence was provided by analyzing extracts from 10 extant bird species. Two suitable options have been identified. The combination of VGPIGPAGNR and VGPIGAAGNR (pheasant only) covers all investigated birds and was not found in other species. The peptide EGPVGFpGADGR covers all investigated birds, but also occurs in several species of crocodiles and turtles. The presence of the generic peptide (combination) was confirmed in food products, proving the principle, and can therefore be used to detect the presence of bird. Furthermore, it is shown how the use of constructed ancestor sequences could benefit the field of paleoproteomics, in the interpretation of collagen MS/MS spectra of ancient species. Our theoretical analysis and assessment of reported Brachylophosaurus canadensis collagen 1α2 MS/MS data provided support for several previous peptide sequence assignments, but we also propose that our constructed ancestral bird sequence GPpGESGAVGPAGPIGSR may fit the MS/MS data better than the original assignment GLPGESGAVGPAGPpGSR.

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Impact of Endotoxins in Gelatine Hydrogels on Chondrogenic Differentiation and Inflammatory Cytokine Secretion In Vitro

Groen

Utomo

Castilho

et al. 2020

IJMS

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Gelatine methacryloyl (GelMA) hydrogels are widely used in studies aimed at cartilage regeneration. However, the endotoxin content of commercially available GelMAs and gelatines used in these studies is often overlooked, even though endotoxins may influence several cellular functions. Moreover, regulations for clinical use of biomaterials dictate a stringent endotoxin limit. We determined the endotoxin level of five different GelMAs and evaluated the effect on the chondrogenic differentiation of equine mesenchymal stromal cells (MSCs). Cartilage-like matrix production was evaluated by biochemical assays and immunohistochemistry. Furthermore, equine peripheral blood mononuclear cells (PBMCs) were cultured on the hydrogels for 24 h, followed by the assessment of tumour necrosis factor (TNF)-α and C–C motif chemokine ligand (CCL)2 as inflammatory markers. The GelMAs were found to have widely varying endotoxin content (two with >1000 EU/mL and three with <10 EU/mL), however, this was not a critical factor determining in vitro cartilage-like matrix production of embedded MSCs. PBMCs did produce significantly higher TNF-α and CCL2 in response to the GelMA with the highest endotoxin level compared to the other GelMAs. Although limited effects on chondrogenic differentiation were found in this study, caution with the use of commercial hydrogels is warranted in the translation from in vitro to in vivo studies because of regulatory constraints and potential inflammatory effects of the content of these hydrogels.

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Gelatin

Cited by 3 publications

References 32 publications

Effect of Pork Skin Gelatin on the Physical Properties of Pork Myofibrillar Protein Gel and Restructured Ham with Microbial Transglutaminase

Effect of Pork Skin Gelatin on the Physical Properties of Pork Myofibrillar Protein Gel and Restructured Ham with Microbial Transglutaminase

The quest for a generic bird target to detect the presence of bird in food products and considerations for paleoprotein analysis

Impact of Endotoxins in Gelatine Hydrogels on Chondrogenic Differentiation and Inflammatory Cytokine Secretion In Vitro

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