ArticleBiotechnology letters2021
Differential proteomics reveals main determinants for the improved pectinase activity in UV-mutagenized Aspergillus niger strain.
Article in Biotechnology letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 5 citations in OpenAlex.
- From the bench to the reactor: engineered filamentous fungi for biochemical and biomaterial production.Biotechnology for biofuels and bioproducts · 2025Review
- Ecuadorian Cacao Mucilage as a Novel Culture Medium Ingredient: Unveiling Its Potential for Microbial Growth and Biotechnological Applications.Foods (Basel, Switzerland) · 2025Article
- Fungal pectinases: an insight into production, innovations and applications.World journal of microbiology & biotechnology · 2023Review
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Authors and funding
9 authors at 1 institution in 1 country.
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Abstract
objectivesTo reveal the potential mechanism and key determinants that contributed to the improved pectinase activity in Aspergillus niger mutant EIMU2, which was previously obtained by UV-mutagenesis from the wild-type A. niger EIM-6.
resultsProteomic analysis for Aspergillus niger EIMU2 by two-dimensional electrophoresis demonstrated that mutant EIMU2 harbored a multiple enzyme system for the degradation of pectin, mainly constituting by main-chain-cleaving enzymes polygalacturonase, pectate lyase, pectinesterase, and some accessory enzymes rhamnogalacturonan lyase and arabinofuranosidase. Further quantitatively differential proteomic analysis revealed that the quantities of four proteins, pectinesterase, rhamnogalacturonan lyase A, DNA-directed RNA polymerase A, and a hypothetical protein in strain EIMU2 were much higher than those in EIM-6. PCR amplification, sequencing and alignment analysis of genes for the two main members of pectin-degrading enzymes, pectate lyase and polygalacturonase showed that their sequences were completely consistent in A. niger EIM-6 and mutant EIMU2.
conclusionsThe result demonstrated that the improved pectinase activity by UV-mutagenesis in A. niger EIMU2 was probably contributed to the up-regulated expression of rhamnogalacturonan lyase, or pectinesterase, which resulted in the optimization of synergy amongst different components of pectin-degrading enzymes.
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