Improved thermal-stability and mechanical properties of type I collagen by crosslinking with casein, keratin and soy protein isolate using transglutaminase

Wu, Xiaomeng; Liu, Yaowei; Liu, Anjun; Wang, Wenhang

doi:10.1016/j.ijbiomac.2017.01.127

Cited by 119 publications

(68 citation statements)

References 44 publications

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“…The thermograms of DSC analysis and the related peak temperatures were given and illustrated in Figure 3. It was reported that the first endothermic events were glass transition, followed by an endotherm associated with the melting of the ordered structures [20,49]. As observed in Figure 3, the value of the pure collagen film (55.63 ∘ C) is inferior to CS1 (85.31 ∘ C), CS2 (103.71 ∘ C), and CS3 (80.71 ∘ C).…”

Section: Thermal Propertiesmentioning

confidence: 81%

“…It suggested that the thermal stability of the CS films has been enhanced, owing to the addition of SA. That may be explained by the increase of interactions provided by SA, stabilizing the collagen structure against unfolding and requiring a higher temperature to degrade collagen [18,20]. Nevertheless, the value for the CS films initially increased and then decreased, with the SA concentration increase.…”

Section: Thermal Propertiesmentioning

confidence: 99%

“…It gained more significance, which offers real potential for applications in the food industry due to its physicochemical properties, short time biodegradability, and nontoxicity. Several authors have developed films or coatings based on collagen to preserve food in laboratory scale [15][16][17][18][19][20]. Nevertheless, since now, scale-up collagenbased films were not successfully produced, as would limit their application in food preservation field.…”

Section: Introductionmentioning

confidence: 99%

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Scale-Up Preparation and Characterization of Collagen/Sodium Alginate Blend Films

Wang

2017

Journal of Food Quality

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In an effort to produce scale-up of edible films, collagen-based films including different amounts of sodium alginate (CS) were prepared by casting method. Films were characterized based on their rheological, thermal, and mechanical properties, water vapor permeability (WVP), and oxygen permeability (OP). The microstructures were also evaluated by scanning electron microscopy (SEM), atomic force microscopy (AFM), and Fourier transform-infrared spectroscopy (FTIR). Furthermore, the addition of sodium alginate effectively improved the viscosity and thermal stability, significantly increased TS, and decreased and WVP ( < 0.05), but with no obvious effect on OP ( > 0.05). SEM and AFM showed homogeneous matrix, with no signs of phase separation in the blends. Overall, films (CS2) produced using collagen (g) : sodium alginate (g) = 10 : 2 showed suitable rheological property (apparent viscosity was 4.87 m Pa s −1 ) and better TS (26.49 Mpa), (64.98%), WVP (1.79 × 10 −10 g⋅cm −1 ⋅s −1 ⋅Pa −1 ), and OP (3.77 × 10 −5 cm 3 ⋅m −2 ⋅d −1 ⋅Pa −1 ).

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Section: Thermal Propertiesmentioning

confidence: 81%

Section: Thermal Propertiesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Scale-Up Preparation and Characterization of Collagen/Sodium Alginate Blend Films

Wang

2017

Journal of Food Quality

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“…acylamino I) referring to CO stretching vibration, 1590–1500 cm −1 (i.e. acylamino II) referring to CN stretching or NH bending vibration, 1300–1000 cm −1 referring to CO stretching vibrations, 1490–1400 cm −1 referring to CO stretching vibrations, and 3500–3000 cm −1 referring to OH stretching or NH bending vibration . Owing to the three proteins additions, the existence of the distinct conformational changes were seen in FTIR spectra.…”

Section: Resultsmentioning

confidence: 99%

“…CN, KRT and SPI all have high heat stability and can be crosslinked by TGase . According to our previous research on type I collagen or collagen fiber with CN, KRT or SPI addition, the films produced all obtained a stable construction, higher thermostability and greater mechanical property via crosslinking action using TGase . Therefore, we chose CN, KRT and SPI as additions loaded to TGase crosslinked collagen fiber (CColF) and then manufactured films.…”

Section: Introductionmentioning

confidence: 99%

Improved structure‐stability and packaging characters of crosslinked collagen fiber‐based film with casein, keratin and SPI

Luo

Liu

et al. 2019

J Sci Food Agric

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Background To improve the structure‐stability and packing characters of collagen fiber, we manufactured crosslinked collagen fiber (CColF)‐based edible films using transglutaminase (TGase). Then we made a comparison on structure‐stability and packing characteristics among the CColF‐based films loaded with casein (CN), keratin (KRT) and soy protein isolate (SPI), respectively. Results Observed from scanning electron microscopy (SEM), the CColF loaded with CN, KRT and SPI showed some unique morphology of the additional proteins. The CColF–protein films performed better packing characteristics including barrier properties, mechanical properties and thermal‐stability properties, compared with CColF films. Importantly, with 500 g kg−1 CN (of CColF) addition, CColF‐based films possessed a greater thermal stability than the other films judged from differential scanning calorimetry (DSC). Meanwhile, the CColF loaded with 100 g kg−1 CN provided a higher value of tensile strength (TS) and the CColF loaded with 100 g kg−1 KRT showed a higher value in elongation‐at‐break (EAB) than the other films. Conclusion In conclusion, the collagen fiber‐based edible films with better structure‐stability and packing characteristics for food packaging was obtained which could be an advantage to promote the development of the application of collagen in packing products. © 2019 Society of Chemical Industry

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Stabilization of oil‐in‐water emulsion gels by pH‐induced electrostatic interactions between soybean protein isolate microgel particles and xanthan gum

Mao,

Cui,

Meng

2024

J Americ Oil Chem Soc

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In this paper, a colloidal dispersion at different pH containing soybean protein isolate (SPI) microgel particles and xanthan gum (XG) was used as the aqueous phase to prepare O/W emulsion gels with soybean oil. Properties of SPI microgel particles were analyzed by particle size, Zeta‐potential, secondary structure, optical contact angle, dynamic interface tension, and SEM testing, respectively. Results showed that pH impact microgels particle size and Zeta‐potential and their emulsification properties. It turned out that only at pH 3, 6, 7, and 8 can construct emulsions successfully. Based on a comparison of microstructure and macroscopic properties, it was found that at pH 3, proteins and polysaccharides were oppositely charged, electrostatic attraction between them reduced proteins located at the interface, and was more likely to form larger droplets, resulting in a bimodal droplet distribution and larger sizes. Conversely, at the pH of 6, 7, and 8, respectively, emulsions exhibited a uniform droplet distribution and more solid‐like rheological properties due to the powerful electrostatic repulsion between SPI and XG. Also, emulsion gels co‐stabilized with proteins and polysaccharides under electrostatic repulsion conditions showed an ideal recovery ability. Overall, this work would be beneficial to the use of emulsion gels in fat substitute systems.

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Improved thermal-stability and mechanical properties of type I collagen by crosslinking with casein, keratin and soy protein isolate using transglutaminase

Cited by 119 publications

References 44 publications

Scale-Up Preparation and Characterization of Collagen/Sodium Alginate Blend Films

Scale-Up Preparation and Characterization of Collagen/Sodium Alginate Blend Films

Improved structure‐stability and packaging characters of crosslinked collagen fiber‐based film with casein, keratin and SPI

Stabilization of oil‐in‐water emulsion gels by pH‐induced electrostatic interactions between soybean protein isolate microgel particles and xanthan gum

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