Laccases are one of many groups of inducible enzymes produced by the filamentous fungus, during colonisation of host plant tissues. While the processes involved in laccase induction are not fully understood, Cupric ions (e.g. CuSO) and gallic acid (GA) have been reported as laccase inducers. This study investigates laccases activities and the expression of three laccase genes () in three isolates grown in laccase-inducing medium (LIM) supplemented with CuSO and GA. Laccase activity in culture filtrates with CuSO increased after 48 h of growth in LIM at 24°C. The induction of transcription was greatest at a concentration of 0.6 mM CuSO, concentrations greater than 0.6 mM inhibited fungal growth. In contrast, no laccase induction was observed in the presence of GA. Liquid chromatography-mass spectroscopy (NanoLC ESI MS/MS) analysis confirmed the presence of a 63.4 kDa protein, the isoform in the culture filtrate with 0.6 mM CuSO. Analysis of mRNA transcripts further showed was also inducible and the expression of and was isolate-dependent. In conclusion, CuSO induces a 63.4 kDa laccase in by induced transcription of the gene.
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http://dx.doi.org/10.1080/21501203.2020.1725677 | DOI Listing |
BMC Plant Biol
January 2025
Forest Pathology Research Lab, Faculty of Agriculture and Forestry, Department of Forest Sciences, University of Helsinki, Helsinki, 00790, Finland.
Background: Mutualistic mycorrhiza fungi that live in symbiosis with plants facilitates nutrient and water acquisition, improving tree growth and performance. In this study, we evaluated the potential of mutualistic fungal inoculation to improve the growth and disease resistance of Scots pine (Pinus sylvestris L.) against the forest pathogen Heterobasidion annosum.
View Article and Find Full Text PDFMolecules
November 2024
Dr. Ikram ul Haq Institute of Industrial Biotechnology, GC University, Lahore 54600, Pakistan.
The aim of the present research was the efficient degradation of industrial textile wastewater dyes using a very active cloned laccase enzyme. For this purpose, potent laccase-producing bacteria were isolated from soil samples collected from wastewater-replenished textile sites in Punjab, Pakistan. The laccase gene from locally isolated strain LI-81, identified as , was cloned into vector pET21a, which was further transformed into BL21 codon plus.
View Article and Find Full Text PDFStress Biol
December 2024
College of Horticulture, Northwest A&F University, Yangling, Shaanxi, 712100, China.
Drought is a prevalent abiotic stress that commonly affects the quality and yield of tea. Although numerous studies have shown that lignin accumulation holds significant importance in conferring drought tolerance to tea plants, the underlying molecular regulatory mechanisms governing the tea plant's response to drought remain largely elusive. LACCASEs (LACs), which belong to the class of plant copper-containing polyphenol oxidases, have been widely reported to participate in lignin biosynthesis in plants and are implicated in numerous plant life processes, especially in the context of adverse conditions.
View Article and Find Full Text PDFFood Res Int
November 2024
School of Food Science and Technology, Jiangnan University, Wuxi 214122, China. Electronic address:
In this study, three types of whey protein isolate (WPI)-tannic acid (TA) covalent conjugates (WPI-TA) were synthesized via alkaline treatment, free radical-induced method, and laccase induction. These conjugates were subsequently utilized in the antisolvent precipitation method to encapsulate pterostilbene (Pte). The structural and functional properties of these conjugates as carriers for intestinal-targeted Pte delivery were thoroughly evaluated.
View Article and Find Full Text PDFPhysiol Mol Biol Plants
October 2024
Laboratory of Morphogenesis, Centre of Advance Study, Department of Botany, Institute of Science, Banaras Hindu University (BHU), Varanasi, Uttar Pradesh 221005 India.
Unlabelled: This study explores the gene () family along with expression in hairy roots of . 42 were identified by detecting three conserved domains: Cu-oxidase, Cu oxidase-2, and Cu oxidase-3. The physicochemical properties show that AaLacs are proteins with 541-1075 amino acids.
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