A Laccase Associated with Lignification in Loblolly Pine Xylem

Science (Impact Factor: 33.61). 05/1993; 260(5108):672-4. DOI: 10.1126/science.260.5108.672
Source: PubMed


Peroxidase has been thought to be the only enzyme that oxidizes monolignol precursors to initiate lignin formation in plants. A laccase was purified from cell walls of differentiating xylem of loblolly pine and shown to coincide in time and place with lignin formation and to oxidize monolignols to dehydrogenation products in vitro. These results suggest that laccase participates in lignin biosynthesis and therefore could be an important target for genetic engineering to modify wood properties or to improve the digestibility of forage crops.

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Available from: Ronald Sederoff, Apr 01, 2014
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    • "Chronological Development of Laccase Applications to Fiberboard Fabrication Reference Novelty Application Yoshida (1883) Discovered laccase Discovered for the first time in latex from the Japanese lacquer tree (Rhus vernicifera) Yamaguchi et al. (1992) phenol dehydrogenative polymerization Achieved bonding among woody-fibers by polymerisation Bao et al. (1993) "
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    ABSTRACT: In the last two decades, laccases have received much attention from researchers because of their specific ability to oxidize lignin. This function of laccase is very useful for applications in several biotechnological processes, including delignification in the pulp and paper industry and the detoxification of industrial effluents from the textile and petrochemical industries. This review focuses on laccase-mediated fiberboard synthesis. Growing concerns regarding the emission of formaldehyde from wood composites has prompted industrialists to consider the fabrication of green composites. Laccase-mediated fiber treatments oxidize the lignin component without affecting the cellulose structure. As a result, free radicals are generated on the fiber surface, and these can act as potential reactive sites for further cross-linking reactions in board manufacturing. Binderless fiberboards prepared using such methods can be considered as green composites because the manufacturing process involves no additional resin.
    Bioresources 07/2015; 10(3):6262-6284. DOI:10.15376/biores.10.3.Nasir · 1.43 Impact Factor
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    • "It will be interesting to see whether the assembly of lignin polymerization complex by CASPs or CASP-like proteins observed in the formation of Casparian strip is a general feature that applies to other types of lignifying cells. Similar to peroxidase, laccase (p-diphenol:dioxygen oxidoreductase , EC also oxidizes monolignols in vitro (Bao et al., 1993; Freudenberg, 1959; Richardson et al., 1997; Sterjiades et al., 1992; Takahama, 1995), and laccase-like activities have been detected in the lignifying cell walls of differentiating xylem (Bao et al., 1993; Driouich et al., 1992; Liu et al., 1994; Richardson et al., 2000). Laccases are coppercontaining extracellular glycoproteins that require O 2 as secondary substrate to oxidize various phenolic, inorganic, and/or aromatic amine substrates (Reinhammar and Malmstroem, 1981). "
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    ABSTRACT: Increased global interest in a bio-based economy has reinvigorated the research on the cell wall structure and composition in plants. In particular, the study of plant lignification has become a central focus, with respect to its intractability and negative impact on the utilization of the cell wall biomass for producing biofuels and bio-based chemicals. Striking progress has been achieved in the last few years both on our fundamental understanding of lignin biosynthesis, deposition and assembly, and on the interplay of lignin synthesis with the plant growth and development. With the knowledge gleaned from basic studies, researchers are now able to invent and develop elegant biotechnological strategies to sophisticatedly manipulate the quantity and structure of lignin and thus to create economically viable bioenergy feedstocks. These concerted efforts open an avenue for the commercial production of cost-competitive biofuel to meet our energy needs.
    Plant Biotechnology Journal 09/2014; 12(9). DOI:10.1111/pbi.12250 · 5.75 Impact Factor
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    • "The liquid medium was prepared according to Tien and Krik [21]. Additional Cu 2+ (final concentration of 0.05 ␮M) was added into the liquid medium to induce the laccase production [22]. Protein purification was performed according to the method reported by Endo et al. [23]. "
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    ABSTRACT: Laccases or laccase-like multicopper oxidases (LMCOs) could catalyze the oxidation of various substrates coupled to the reduction of oxygen to water. In this study, eight strains with laccase activity were isolated from composting samples in different phases, among which strain C1 isolated from the thermophilic-phase sample presented the highest laccase activity. The purified LMCO of strain C1 showed a single protein band on SDS-PAGE gel with a molecular mass of about 38 kDa. The novel laccase showed alkaline resistance and moderate thermostability. The enzyme activity was activated by some metal ions such as Cu2+, Co2+ and Fe3+ at the concentration of 1 mM, while was strongly inhibited in the presence of Hg2+. The LMCO could efficiently decolorize the indigo carmine and diamond black PV with syringaldehyde as mediator, which suggested a great potential for dye decolorization in the textile industry. The novel strain was identified as Streptomyces sp. C1. The finding of new laccase-producing Streptomyces sp. C1 in this study will also contribute to the further explanation of the function of Actinomycetes in the thermophilic phase of composting.
    Biochemical Engineering Journal 03/2013; 72:70–76. DOI:10.1016/j.bej.2013.01.004 · 2.47 Impact Factor
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