Moderate laccase-crosslinking improves the mechanical and thermal properties of acid-swollen collagen-based films modified by gallotannins. (September 2020)
- Record Type:
- Journal Article
- Title:
- Moderate laccase-crosslinking improves the mechanical and thermal properties of acid-swollen collagen-based films modified by gallotannins. (September 2020)
- Main Title:
- Moderate laccase-crosslinking improves the mechanical and thermal properties of acid-swollen collagen-based films modified by gallotannins
- Authors:
- Duan, Songmei
Wang, Wenhang
Li, Shuzhi
Zhang, Kai
Guo, Yang
Ma, Yunhao
Zhao, Kaixuan
Li, Yu - Abstract:
- Abstract: Using enzymatical crosslinking as a potential chemical-bonding alternative to improve collagen materials' properties is a challenge due to its relatively low efficiency. Here, the laccase-mediator system (LMS) with gallotannin (GT) as a mediator was introduced to acid-swollen collagen (ASC) films for its reinforcement. Hypothetically, laccase (Lac) in LMS oxidize GT to reactive quinone, which can attack ASC more easily compared to the direct catalyzation of Lac, resulting in an efficient crosslinking and related performance of ASC. We found that films with Lac from 3 to 12 U/g had increasing tensile strength (33.42 ± 2.30 to 44.82 ± 3.85 MPa), and with further addition of low-dose GT (0.1 mg/g) showed higher tensile strength (39.06 ± 6.25 to 45.33 ± 3.37 MPa). Meantime, denaturation temperature of Lac films gradually raised from 99.42 °C to 103.05 °C and those of GT-Lac films were higher ranging from 102.67 °C to 109.07 °C. We also observed that GT-Lac films presented smoother surfaces and more compact laminar cross-sections than those of Lac films, of which this excellent structure generally accompanied with low water wettability resulting from preventing water to penetrate the films. Moreover, the amide Ⅱ and Ⅲ peaks of GT-Lac films shifted to lower wavenumbers than those of Lac films, along with a less proportion of random coils (%) of ASC, partially supporting the hypothesis of LMS's crosslinking. In summary, the GT-contained LMS provides the potential toAbstract: Using enzymatical crosslinking as a potential chemical-bonding alternative to improve collagen materials' properties is a challenge due to its relatively low efficiency. Here, the laccase-mediator system (LMS) with gallotannin (GT) as a mediator was introduced to acid-swollen collagen (ASC) films for its reinforcement. Hypothetically, laccase (Lac) in LMS oxidize GT to reactive quinone, which can attack ASC more easily compared to the direct catalyzation of Lac, resulting in an efficient crosslinking and related performance of ASC. We found that films with Lac from 3 to 12 U/g had increasing tensile strength (33.42 ± 2.30 to 44.82 ± 3.85 MPa), and with further addition of low-dose GT (0.1 mg/g) showed higher tensile strength (39.06 ± 6.25 to 45.33 ± 3.37 MPa). Meantime, denaturation temperature of Lac films gradually raised from 99.42 °C to 103.05 °C and those of GT-Lac films were higher ranging from 102.67 °C to 109.07 °C. We also observed that GT-Lac films presented smoother surfaces and more compact laminar cross-sections than those of Lac films, of which this excellent structure generally accompanied with low water wettability resulting from preventing water to penetrate the films. Moreover, the amide Ⅱ and Ⅲ peaks of GT-Lac films shifted to lower wavenumbers than those of Lac films, along with a less proportion of random coils (%) of ASC, partially supporting the hypothesis of LMS's crosslinking. In summary, the GT-contained LMS provides the potential to greenly modify collagenous materials extensively used in food industry, especially meat processing. Graphical abstract: Image 1 Highlights: Laccase (Lac) successfully crosslinked acid-swollen collagen (ASC) film. The crosslinking efficiency of Lac was dose-dependent. Co-adding gallotannins (GT) enhanced some properties of film. GT-Lac film had higher dry tensile modulus and strength than commercial casing. … (more)
- Is Part Of:
- Food hydrocolloids. Volume 106(2020)
- Journal:
- Food hydrocolloids
- Issue:
- Volume 106(2020)
- Issue Display:
- Volume 106, Issue 2020 (2020)
- Year:
- 2020
- Volume:
- 106
- Issue:
- 2020
- Issue Sort Value:
- 2020-0106-2020-0000
- Page Start:
- Page End:
- Publication Date:
- 2020-09
- Subjects:
- Laccase -- Crosslinking -- Redox reaction -- LMS -- Gallotannins -- Mediator
Hydrocolloids -- Periodicals
Food additives -- Periodicals
Colloïdes -- Périodiques
Aliments -- Additifs -- Périodiques
Colloids
Food additives
Periodicals
Electronic journals
664.06 - Journal URLs:
- http://www.sciencedirect.com/science/journal/0268005X ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodhyd.2020.105917 ↗
- Languages:
- English
- ISSNs:
- 0268-005X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.556000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 13375.xml