Enzymatic cross-linking of ferulated arabinoxylan: effect of laccase or peroxidase catalysis on the gel characteristics

被引:0
|
作者
Ana L. Martínez-López
Elizabeth Carvajal-Millan
Jorge Marquez-Escalante
Alma C. Campa-Mada
Agustín Rascón-Chu
Yolanda L. López-Franco
Jaime Lizardi-Mendoza
机构
[1] Centro de Investigación en Alimentación y Desarrollo,
来源
关键词
Polysaccharides; Enzymes; Gelation; Ferulic acid; Swelling;
D O I
暂无
中图分类号
学科分类号
摘要
Arabinoxylans (AX) gels at 4% (w/v) were prepared using laccase (LAX gels) or peroxidase (PAX gels), and their cross-linking, rheological, structural, and spectroscopic characteristics were investigated. LAX gels presented lower amount of 5,5′-diferulic acid (11%), smaller mesh size (128 nm), and higher hardness (37 N) and elasticity (430 Pa) than the PAX gels (28%, 197 nm, 7 N, and 120 Pa, respectively). Microscopy of the LAX gels showed linked strands, while the system was less connected in the PAX gels. The Raman band at 2895 cm−1 of the LAX and PAX gels was less intense, indicating enhanced hydrogen bonding compared to that of AX. This decrease was less dramatic for the PAX gels. The greater content of 5,5′-diferulic acid in PAX gels could favor intrachain bonds, affecting their rheological, structural, and spectroscopic characteristics. Laccase may be a better option than peroxidase for AX gelation intended for food and biotechnological applications.
引用
收藏
页码:311 / 318
页数:7
相关论文
共 50 条
  • [21] Syneresis in Gels of Highly Ferulated Arabinoxylans: Characterization of Covalent Cross-Linking, Rheology, and Microstructure
    Morales-Burgos, Ana M.
    Carvajal-Millan, Elizabeth
    Lopez-Franco, Yolanda L.
    Rascon-Chu, Agustin
    Lizardi-Mendoza, Jaime
    Sotelo-Cruz, Norberto
    Brown-Bojorquez, Francisco
    Burgara-Estrella, Alexel
    Pedroza-Montero, Martin
    POLYMERS, 2017, 9 (05):
  • [22] Physicochemical Properties of Pectin Modified by Cross-Linking with Ferulic Acid under the Catalysis of Horseradish Peroxidase
    Liu Y.
    Li X.
    Liu G.
    Li J.
    Yan S.
    Shipin Kexue/Food Science, 2020, 41 (14): : 9 - 14
  • [23] Yoghurt gel formation by means of enzymatic protein cross-linking during microbial fermentation
    Bonisch, Martin P.
    Huss, Manfred
    Lauber, Sabine
    Kulozik, Ulrich
    FOOD HYDROCOLLOIDS, 2007, 21 (04) : 585 - 595
  • [24] Catalysis by Au@pNIPAM Nanocomposites: Effect of the Cross-Linking Density
    Carregal-Romero, Susana
    Buurma, Niklaas J.
    Perez-Juste, Jorge
    Liz-Marzan, Luis M.
    Herves, Pablo
    CHEMISTRY OF MATERIALS, 2010, 22 (10) : 3051 - 3059
  • [25] Enzymatic Cross-Linking of a Nanofibrous Peptide Hydrogel
    Bakota, Erica L.
    Aulisa, Lorenzo
    Galler, Kerstin M.
    Hartgerink, Jeffrey D.
    BIOMACROMOLECULES, 2011, 12 (01) : 82 - 87
  • [26] Cross-linking of whey proteins by enzymatic oxidation
    Færgemand, M
    Otte, J
    Qvist, KB
    JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1998, 46 (04) : 1326 - 1333
  • [27] ENZYMATIC AND NONENZYMATIC CROSS-LINKING OF COLLAGEN AND ELASTIN
    REISER, K
    MCCORMICK, RJ
    RUCKER, RB
    FASEB JOURNAL, 1992, 6 (07): : 2439 - 2449
  • [28] Selective cross-linking of coinciding protein assemblies by in-gel cross-linking mass spectrometry
    Hevler, Johannes F.
    Lukassen, Marie, V
    Cabrera-Orefice, Alfredo
    Arnold, Susanne
    Pronker, Matti F.
    Franc, Vojtech
    Heck, Albert J. R.
    EMBO JOURNAL, 2021, 40 (04):
  • [29] Cross-linking of casein by peroxidase and modification in emulsifying properties
    Key Lab of Dairy Science, Northeast Agricultural University, Harbin 150030, China
    Nongye Jixie Xuebao, 2009, 11 (144-149):
  • [30] Effect of cross-linking density on swelling behavior of NIPA gel particles
    Oh, KS
    Oh, JS
    Choi, HS
    Bae, YC
    MACROMOLECULES, 1998, 31 (21) : 7328 - 7335