Production of Oligosaccharides by Fungi or Fungal Enzymes

The chemical factors that regulate the synthesis of resveratrol (RV) in filamentous fungi are still unknown. This work reports on the RV production by Arcopilus aureus MaC7A under controlled conditions and the effect of amino acid precursors (PHE and TYR), monoterpenes (limonone, camphor, citral, thymol, menthol), and mixtures of hydrolytic enzymes (Glucanex) as elicitors for boosting fungal RV. Batch cultures with variable concentrations of PHE and TYR (50–500 mg L−1) stimulated RV production from 127.9 ± 4.6 to 221.8 ± 5.2 mg L−1 in basic cultures developed in PDB (pH 7) added with 10 g L−1 peptone at 30 °C. Maximum levels of RV and biomass were maintained during days 6–8 under these conditions, whereas a dramatic RV decrease was observed from days 10–12 without any loss of biomass. Among the tested volatiles, citral (50 mg L−1) enhanced RV production until 187.8 ± 2.2 mg L−1 in basic cultures, but better results were obtained with Glucanex (100 mg L−1; 198.3 ± 7.6 mg L−1 RV). Optimized batch cultures containing TYR (200 mg L−1), citral (50 mg L−1), thymol (50 mg L−1), and Glucanex (100 mg L−1) produced up to 237.6 ± 4.7 mg L−1 of RV. Our results suggest that low concentrations of volatiles and mixtures of isoenzymes with β-1, 3 glucanase activity increase the biosynthesis of fungal RV produced by A. aureus MaC7A in batch cultures.

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Biotechnological Applications of Fungal Enzymes with Special Reference to Bioremediation

Environmental Biotechnology Vol. 2 - Environmental Chemistry for a Sustainable World ◽

10.1007/978-3-030-38196-7_10 ◽

2020 ◽

pp. 221-247

Author(s):

Madan L. Verma ◽

Meenu Thakur ◽

Jatinder S. Randhawa ◽

Deepka Sharma ◽

Akhilesh Thakur ◽

...

Keyword(s):

Special Reference ◽

Biotechnological Applications ◽

Fungal Enzymes

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Commercial Importance of Some Fungal Enzymes

Handbook of Fungal Biotechnology - Mycology ◽

10.1201/9780203027356.ch22 ◽

2003 ◽

Author(s):

Rajendra Saxsena ◽

Bhawana Malhotra ◽

Anoop Batra

Keyword(s):

Fungal Enzymes ◽

Commercial Importance

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Formation of Oxygenated Fatty Acids by Fungal Enzymes

Lipid Biotechnology ◽

10.1201/9780203908198.ch14 ◽

2002 ◽

Author(s):

Chao Su ◽

Ernst Oliw

Keyword(s):

Fatty Acids ◽

Fungal Enzymes ◽

Oxygenated Fatty Acids

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Chemoenzymatic Synthesis of Complex Phenylpropanoid Derivatives by the Botrytis cinerea Secretome and Evaluation of Their Wnt Inhibition Activity

Frontiers in Plant Science ◽

10.3389/fpls.2021.805610 ◽

2022 ◽

Vol 12 ◽

Author(s):

Robin Huber ◽

Laurence Marcourt ◽

Alexey Koval ◽

Sylvain Schnee ◽

Davide Righi ◽

...

Keyword(s):

Botrytis Cinerea ◽

State Of The Art ◽

Chemoenzymatic Synthesis ◽

Preparative Hplc ◽

Spectroscopic Methods ◽

Inhibition Activity ◽

Fungal Enzymes ◽

First Time ◽

Compound Series ◽

Phenylpropanoid Derivatives

In this study, a series of complex phenylpropanoid derivatives were obtained by chemoenzymatic biotransformation of ferulic acid, caffeic acid, and a mixture of both acids using the enzymatic secretome of Botrytis cinerea. These substrates were incubated with fungal enzymes, and the reactions were monitored using state-of-the-art analytical methods. Under such conditions, a series of dimers, trimers, and tetramers were generated. The reactions were optimized and scaled up. The resulting mixtures were purified by high-resolution semi-preparative HPLC combined with dry load introduction. This approach generated a series of 23 phenylpropanoid derivatives, 11 of which are described here for the first time. These compounds are divided into 12 dimers, 9 trimers (including a completely new structural scaffold), and 2 tetramers. Elucidation of their structures was performed with classical spectroscopic methods such as NMR and HRESIMS analyses. The resulting compound series were analyzed for anti-Wnt activity in TNBC cells, with several derivatives demonstrating specific inhibition.

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Short Communication: The higher laccase enzyme producer, Cerrena sp. BMd.TA.1, isolated from Gunung Rinjani National Park, West Nusa Tenggara, Indonesia

Biodiversitas Journal of Biological Diversity ◽

10.13057/biodiv/d210853 ◽

2020 ◽

Vol 21 (8) ◽

Author(s):

SARAH ASIH FAULINA ◽

ASEP HIDAYAT ◽

SYAMSUL FALAH ◽

Apri Heri Iswanto

Keyword(s):

Manganese Peroxidase ◽

National Park ◽

Short Communication ◽

Industrial Effluent ◽

Fungal Enzymes ◽

Fungal Laccase ◽

Synthetic Dye ◽

Environmental Friendly ◽

Laccase Enzyme ◽

High Level

Abstract. Faulina SA, Irfani M, Falah S, Hidayat A, Iswanto AH. 2020. Short Communication: The higher laccase enzyme producer, Cerrena sp. BMd. TA.1, isolated from Gunung Rinjani National Park, West Nusa Tenggara, Indonesia. Biodiversitas 21: 3837-3842. Lies in the Wallace line, Gunung Rinjani National Park (GRNP) offers unique biodiversity, fungi included. Fungal enzymes have been unceasingly searched and studied for various applications, particularly for biodegradation. Fungal laccase enzyme showed prospective environmental-friendly approach in treating industrial effluent, remazol brilliant blue R (RBBR) which is used as a synthetic dye. This study aimed to explore the laccase-producing fungi from the GNRP, as well as investigate their ability in decolorizing RBBR. The study discovered that the most prospective fungi isolate, molecularly identified as Cerrena sp. BMd.TA.1, produced a high level of laccase (> 2300 U mL-1) and manganese peroxidase (MnP, 300 U mL-1). In the application of this isolate, the laccase showed as predominant enzyme in RBBR decolorization process and the RBBR could be decolorized more than 80% at 24 h reaction. It suggested that Cerrena sp BMd.TA.1 isolate is highly potential as laccase enzyme producer and may be considered for further investigations in its applications for biodegradation, especially of dyes effluent.

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Biochemical characterization of a glycoside hydrolase family 43 β-D-galactofuranosidase from the fungus Aspergillus niger

10.1101/2021.10.27.466152 ◽

2021 ◽

Author(s):

Gregory S Bulmer ◽

Fang Wei Yuen ◽

Naimah Begum ◽

Bethan S Jones ◽

Sabine S Flitsch ◽

...

Keyword(s):

Aspergillus Niger ◽

Glycoside Hydrolase ◽

Biochemical Characterization ◽

Maximum Activity ◽

Glycoside Hydrolase Family ◽

Enzyme Specificity ◽

Fungal Enzymes ◽

Glycoside Hydrolase Family 43 ◽

Hydrolase Family

β-D-Galactofuranose (Galf) and its polysaccharides are found in bacteria, fungi and protozoa but do not occur in mammalian tissues, and thus represent a specific target for anti-pathogenic drugs. Understanding the enzymatic degradation of these polysaccharides is therefore of great interest, but the identity of fungal enzymes with exclusively galactofuranosidase activity has so far remained elusive. Here we describe the identification and characterization of a galactofuranosidase from the industrially important fungus Aspergillus niger. Phylogenetic analysis of glycoside hydrolase family 43 subfamily 34 (GH43_34) members revealed the occurrence of three distinct clusters and, by comparison with specificities of characterized bacterial members, suggested a basis for prediction of enzyme specificity. Using this rationale, in tandem with molecular docking, we identified a putative β-D-galactofuranosidase from A. niger which was recombinantly expressed in Escherichia coli. The Galf-specific hydrolase, encoded by xynD demonstrates maximum activity at pH 5, 25 °C towards 4-Nitrophenyl-β-galactofuranoside (pNP-βGalf), with a Km of 17.9 ± 1.9 mM and Vmax of 70.6 ± 5.3 μmol min-1. The characterization of this first fungal GH43 galactofuranosidase offers further molecular insight into the degradation of Galf-containing structures and may inform clinical treatments against fungal pathogens.

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