laccase has been researched along with 1-phenylpropanol* in 2 studies
2 other study(ies) available for laccase and 1-phenylpropanol
| Article | Year |
|---|---|
Laccase isoform diversity in basidiomycete Lentinus strigosus 1566: Potential for phenylpropanoid polymerization.
Three laccase isoforms with different physicochemical properties could be purified from culture liquid of basidiomycete Lentinus strigosus 1566 obtained during submerged cultivation. The purified laccases possessed individual selectivity in relation to different phenolic compounds. Laccases I, II, and III (59, 65, and 61 kDa respectively) were more active in acidic conditions at around 70 °C. However, in contrast to laccases I and II, laccase III retained its activity (8-30%) and stability during at least one week of incubation at neutral conditions that allows its biotechnological application carried out at neutral environment. The activation phenomena for some of the purified laccases from L. strigosus 1566 during incubation at high temperature, different pH, and sulfates is shown and discussed. According to MALDI-TOF analysis, laccases I and II are most closely related to the laccase of Panus rudis (AAR13230). Transformation of phenylpropanoids by the predominant laccases of L. strigosus 1566 to different polymers was demonstrated, indicating a great potential for producing novel pharmaceutical valuable analogues of lignans, stilbenes, flavonoids, and etc.. The studied laccases, which are products of the same strain, can become a convenient model for further studies of the structural mechanisms of the shift of T-/pH-optima, activation, and T-/pH-stability. Topics: Amino Acid Sequence; Basidiomycota; Enzyme Stability; Glycosylation; Hydrogen-Ion Concentration; Isoenzymes; Kinetics; Laccase; Metals; Polymerization; Propanols; Temperature | 2019 |
Laccase GhLac1 Modulates Broad-Spectrum Biotic Stress Tolerance via Manipulating Phenylpropanoid Pathway and Jasmonic Acid Synthesis.
Plants are constantly challenged by a multitude of pathogens and pests, which causes massive yield and quality losses annually. A promising approach to reduce such losses is to enhance the immune system of plants through genetic engineering. Previous work has shown that laccases (p-diphenol:dioxygen oxidoreductase, EC 1.10.3.2) function as lignin polymerization enzymes. Here we demonstrate that transgenic manipulation of the expression of the laccase gene Topics: Animals; Aphids; Cyclopentanes; Disease Resistance; Gene Expression Regulation, Plant; Gossypium; Laccase; Lepidoptera; Lignin; Oxylipins; Plant Diseases; Plant Proteins; Propanols; Verticillium | 2018 |