scholarly journals PROSPECTION OF FILAMENTOUS FUNGI AND THE PRODUCTION OF AMYLASE BY ASPERGILLUS sp. M1.7.2

2020 ◽  
Vol 6 (3) ◽  
pp. 0365-0376
Author(s):  
Mariana Tainná Silva Souza ◽  
Barbhara Mota Marinho ◽  
Thiago Machado Pasin ◽  
David Lee Nelson ◽  
Vivian Machado Benassi
Keyword(s):  
Filamentous Fungi ◽  
Industrial Applications ◽  
Minas Gerais ◽  
Maximum Activity ◽  
Physiological Characteristics ◽  
Enzymatic Characterization ◽  
Culture Parameters ◽  
Aspergillus Sp

Amylases are used in numerous industrial applications for converting starch into products of greater value.  This work aimed to prospect filamentous fungi, analyze the morphological and physiological characteristics of the isolates; as well as to select an amylase producing fungus and to optimize the parameters for the cultivation of the microorganism and biochemically characterize the amylase. Among 21 filamentous fungi isolated in Janaúba, state of Minas Gerais, Brazil, the best amylase producer was selected for standardization of culture parameters and subsequent enzymatic characterization. Maximum activity was obtained in CP medium after six days of cultivation at 30 °C. Amylases produced by this fungus are stable to variations in pH and temperature, exhibited optimum activities at 65 oC and pH 6.0, and were significantly activated in the presence of 5 and 10 mm KH2PO4.

Biotransformation of Coumarins by Filamentous Fungi: An Alternative Way for Achievement of Bioactive Analogs

2019 ◽  
Vol 16 (6) ◽  
pp. 568-577 ◽  
Author(s):  
Jainara Santos do Nascimento ◽  
João Carlos Silva Conceição ◽  
Eliane de Oliveira Silva
Keyword(s):  
Filamentous Fungi ◽  
Chemical Reactions ◽  
Biological Activities ◽  
Chemical Transformations ◽  
Chemical Structures ◽  
Pattern Structures ◽  
Pharmacological Interest ◽  
Aspergillus Sp ◽  
The Impact ◽  
Related Compounds

Coumarins are natural 1,2-benzopyrones, present in remarkable amounts as secondary metabolites in edible and medicinal plants. The low yield in the coumarins isolation from natural sources, along with the difficulties faced by the total synthesis, make them attractive for biotechnological studies. The current literature contains several reports on the biotransformation of coumarins by fungi, which can generate chemical analogs with high selectivity, using mild and eco-friendly conditions. Prompted by the enormous pharmacological interest in the coumarin-related compounds, their alimentary and chemical applications, this review covers the biotransformation of coumarins by filamentous fungi. The chemical structures of the analogs were presented and compared with those from the pattern structures. The main chemical reactions catalyzed the insertion of functional groups, and the impact on the biological activities caused by the chemical transformations were discussed. Several chemical reactions can be catalyzed by filamentous fungi in the coumarin scores, mainly lactone ring opening, C3-C4 reduction and hydroxylation. Chunninghamella sp. and Aspergillus sp. are the most common fungi used in these transformations. Concerning the substrates, the biotransformation of pyranocoumarins is a rarer process. Sometimes, the bioactivities were improved by the chemical modifications and coincidences with the mammalian metabolism were pointed out.

scholarly journals Prospects of Biocatalyst Purification Enroute Fermentation Processes

2021 ◽  
Author(s):  
Michael Bamitale Osho ◽  
Sarafadeen Olateju Kareem
Keyword(s):  
Fermentation Process ◽  
Colloidal Particles ◽  
Methyl Cellulose ◽  
Industrial Applications ◽  
Maximum Activity ◽  
Inorganic Materials ◽  
Organic Substrates ◽  
Ammonium Sulphate Precipitation ◽  
Sodom Apple ◽  
Microbial Agents

Biotransformation of broth through fermentation process suffers a major setback when it comes to disintegration of organic substrates by microbial agents for industrial applications. These biocatalysts are in crude/dilute form hence needs to be purified to remove colloidal particles and enzymatic impurities thus enhancing maximum activity. Several contractual procedures of concentrating dilute enzymes and proteins had been reported. Such inorganic materials include ammonium sulphate precipitation; salting, synthetic polyacrylic acid; carboxy-methyl cellulose, tannic acid, edible gum and some organic solvents as precipitants etc. The emergence of organic absorbents such as sodom apple (Calostropis procera) extract, activated charcoal and imarsil had resulted in making significant impact in industrial circle. Various concentrations of these organic extracts have been used as purifying agents on different types of enzyme vis: lipase, amylase, protease, cellulase etc. Purification fold and stability of the enzyme crude form attained unprecedented results.

A novel Swollenin from Talaromyces leycettanus JCM12802 exhibits cellulase activity and enhanced cellulase hydrolysis towards various substrates

2020 ◽  
Author(s):  
Honghai Zhang ◽  
Yuan Wang ◽  
Roman Brunecky ◽  
Bin Yao ◽  
Xiangming Xie ◽  
...  
Keyword(s):  
Synergistic Effect ◽  
Functional Diversity ◽  
Specific Activity ◽  
Biomass Conversion ◽  
Hydrolytic Enzymes ◽  
Cellulase Activity ◽  
Industrial Applications ◽  
Maximum Activity ◽  
Carbohydrate Binding ◽  
Cell Wall Polysaccharides

Abstract Background Swollenins are present in some fungal species involved in the biodegradation of cellulosic substrates. They appear to promote a rearrangement in the network of non-covalent interactions between the cell wall polysaccharides, thus making it more accessible for degradation by hydrolytic enzymes. Here, we have reported a detailed characterization of a recombinant swollenin with respect to its disruptive activity on cellulosic substrates and synergistic effect with cellulases. Results In the present study, a novel swollenin gene Tlswo consisting of an open reading frame encoding 503 amino acids was identified from Talaromyces leycettanus JCM12802 and successfully expressed in Trichoderma reesei and Pichia pastoris. Similar to other fungal swollenins, TlSWO contained a N-terminal family 1 carbohydrate binding module (CBM1) followed by a Ser/Thr rich linker connected to expansin-like domain which includes a family 45 endoglucanase-like domain and group-2 grass pollen allergen domain. TlSWO demonstrated disruptive activity on Avicel and displayed a high synergistic effect with cellobiohydrolases, enhancing its hydrolytic performance up to 132%. The activity of TlSWO on various substrates and biomass was also examined. It was shown that TlSWO could release reducing sugars from lichenan, barley β-glucan, carboxymethyl cellulose sodium (CMC-Na) and laminarin. The specific activity of TlSWO towards the substates above is 9.0 ± 0.100 U/mg, 8.9 ± 0.100U/mg, 2.3 ± 0.002 U/mg and 0.79 ± 0.002 U/mg respectively. Moreover, TlSWO exhibits maximum activity at pH 4.0 and 50 ℃. Conclusion This study reported on a novel swollenin with highly efficient for biomass conversion. It also reveals the functional diversity of swollenin with activity on various substrates. Although the exact mechanism of swollenin catalytic action activity still remains unknown, the functional diversity of TlSWO makes it a good candidate for industrial applications.

scholarly journals Characterization of a Novel β-Xylosidase, XylC, fromThermoanaerobacterium saccharolyticumJW/SL-YS485

2010 ◽  
Vol 77 (3) ◽  
pp. 719-726 ◽  
Author(s):  
Weilan Shao ◽  
Yemin Xue ◽  
Ailian Wu ◽  
Irina Kataeva ◽  
Jianjun Pei ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Glycosyl Hydrolase ◽  
Gel Filtration ◽  
Industrial Applications ◽  
Maximum Activity ◽  
Site Directed Mutagenesis ◽  
Stem Loop ◽  
Translational Initiation ◽  
Reading Frame ◽  
Gradient Gel Electrophoresis

ABSTRACTThe 1,914-bp open reading frame ofxylCfromThermoanaerobacterium saccharolyticumJW/SL-YS485 encodes a calculated 73-kDa β-xylosidase, XylC, different from any glycosyl hydrolase in the database and representing a novel glycohydrolase family. Hydrolysis occurred under retention of the anomeric configuration, and transglycosylation occurred in the presence of alcohols as acceptors. With the use of vector pHsh, expression of XylC, the third β-xylosidase in this bacterium, increased approximately 4-fold when a loop within the translational initiation region in the mRNA was removed by site-directed mutagenesis. The increased expression ofxylCmis due to removal of a stem-loop structure without a change of the amino acid sequence of the heterologously expressed enzyme (XylCrec). When gel filtration was applied, purified XylC had molecular masses of 210 kDa and 265 kDa using native gradient gel electrophoresis. The protein consisted of 78-kDa subunits based on SDS gel electrophoresis and contained 6% carbohydrates. XylC and XylCrecexhibited maximum activity at 65°C and pH65°C6.0, a 1-h half-life at 67°C, aKmforp-nitrophenyl-β-d-xyloside of 28 mM, and aVmaxof 276 U/mg and retained 70% activity in the presence of 200 mM xylose, suggesting potential for industrial applications.

Natural pigment extraction from five filamentous fungi for industrial applications and dyeing of leather

2010 ◽  
Vol 79 (2) ◽  
pp. 262-268 ◽  
Author(s):  
Palanivel Velmurugan ◽  
Seralathan Kamala-Kannan ◽  
Vellingiri Balachandar ◽  
Perumalsamy Lakshmanaperumalsamy ◽  
Jong-Chan Chae ◽  
...  
Keyword(s):  
Filamentous Fungi ◽  
Industrial Applications ◽  
Natural Pigment ◽  
Pigment Extraction

scholarly journals Transporte, patogenicidade e transmissibilidade de fungos associados às sementes de pinhão manso

2011 ◽  
Vol 33 (4) ◽  
pp. 663-670 ◽  
Author(s):  
Danila Alves Corrêa de Sá ◽  
Gil Rodrigues dos Santos ◽  
Gleiber Quintão Furtado ◽  
Eduardo Andréa Lemus Erasmo ◽  
Ildon Rodrigues do Nascimento
Keyword(s):  
Colletotrichum Gloeosporioides ◽  
Minas Gerais ◽  
Sao Paulo ◽  
São Paulo ◽  
Penicillium Sp ◽  
Fusarium Sp ◽  
Aspergillus Sp ◽  
Rhizopus Sp

Objetivou-se determinar a taxa de transporte de população de fungos associados às sementes de pinhão manso, a patogenicidade desses microrganismos a plântulas e frutos e a transmissibilidade fruto-semente e semente-plântula. Avaliaram-se a taxa de transporte, por meio de blotter test, de sementes produzidas nos estados de Minas Gerais, São Paulo, Bahia e Tocantins. As sementes foram submetidas aos tratamentos: sem desinfestação com tegumento (SDCT), sem desinfestação sem tegumento (SDST), com desinfestação com tegumento (CDCT) e com desinfestação sem tegumento (CDST). A incidência (%) dos fungos foi avaliada sob microscópio estereoscópico binocular. Para o teste de patogenicidade em plântulas e frutos inocularam-se suspensões de 10(6) esporos e discos de BDA com micélio, respectivamente. Para os fungos fitopatogênicos avaliaram-se a transmissibilidade fruto-semente e semente-plântula. O tratamento SDCT permitiu a detecção de maior número de fungos. Os fungos identificados foram Colletotrichum gloeosporioides, C. capsici, Curvularia sp., Verticillium sp., Fusarium sp., Penicillium sp., Aspergillus sp., A. niger e Rhizopus sp. Apenas as espécies de Colletotrichum são patogênicas às plântulas e frutos. Para ambas espécies há transmissibilidade fruto-semente, entretanto não é observada transmissão semente-plântula.

scholarly journals Mortierella verticillata Linnem. (Mortierellomycota, Mortierellales) isolated from mountainous environments: a first report from South America

Check List ◽  
2020 ◽  
Vol 16 (4) ◽  
pp. 901-904
Author(s):  
Camila Melo Gonçalves ◽  
Rafael José Vilela de Oliveira ◽  
Rejane Maria Ferreira da Silva ◽  
Carlos Alberto Fragoso de Souza ◽  
Diogo Xavier Lima ◽  
...  
Keyword(s):  
Sequence Analysis ◽  
South America ◽  
Filamentous Fungi ◽  
Minas Gerais ◽  
The State ◽  
Rdna Sequence ◽  
Its Rdna ◽  
First Report ◽  
Aerial Hyphae ◽  
First Occurrence

During a study on filamentous fungi in the soil of mountainous environments in the state of Minas Gerais, Brazil, one specimen of Mortierella verticillata Linnem. was isolated. Fungal identity was confirmed by morphology and ITS rDNA sequence analysis. This study reports the first occurrence of M. verticillata in South America. This species is distinguished by its monopodial sporangiophores growing on aerial hyphae of verticillate branches, and single-spored sporangia finely ornamented with a diffluent wall. In this manuscript, the specimen is described and illustrated, and the distribution of this species is discussed.

Characterization of L-fucose isomerase from Paenibacillus rhizosphaerae to produce L-fuculose from hydrolyzed fucoidan and commercial fucose

2019 ◽  
Author(s):  
Muhammad Waheed Iqbal ◽  
Tahreem Riaz ◽  
Shahid Mahmood ◽  
Yingying Zhu ◽  
Dawei Ni ◽  
...  
Keyword(s):  
Industrial Applications ◽  
Maximum Activity ◽  
Lysosomal Disease ◽  
Simple Method ◽  
Enzymatic Production ◽  
Native Molecular Mass ◽  
Anti Cancer ◽  
Viral Hepatitis B ◽  
High Production

Abstract Background L-fuculose is an expensive and rare sugar used against different kinds of diseases such as HIV, anti-cancer, anti-viral, Hepatitis-B, human lysosomal disease (fucosidosis), and cardio-protective drugs. The enzymatic way of converting L-fucose into L-fuculose would be an effective method with great industrial applications. The purpose of this research is to introduce a high production of L-fuculose from cheap and natural sources (fucoidan) and commercially source (Sigma-Aldrich) by a recombinant enzyme L-fucose isomerase from Paenibacillus rhizosphaerae (Pa-LFI).Results Fucose containing polysaccharide (FPs) called fucoidan was extracted, hydrolyzed and characterized by U. pinnatifida for enzymatic production of L-fuculose. The FPs provide 35.9% of fucose along with few other monosaccharides. Pa-LFI was characterized and purified with a single band at 65 kDa. It showed an activity of 104.5 U mg -1 and exhibited as a hexamer with native molecular mass 396 kDa. The maximum activity for recombinant Pa-LFI was detected at pH 6.5 and 50 °C in 1 mM of Mn 2+ . The melting temperature observed 75 °C and half-life at 50 °C was 12.6 h. The isomerizing activity of Pa-LFI with aldose substrate (L-fucose) was higher exposing K m , k cat and k cat / K m 86.2 mM, 32831 min -1 and 335 min -1 mM -1 respectively. The conversion ratio of L-fuculose from 100 g L -1 of FPs and commercial fucose after the equilibrium state was about 6% (5.6 g L -1 ) and 30% (30.2 g L -1 ) respectively.Conclusion Pa-LFI catalyzed the reaction to convert L-fucose into L-fuculose. The enzyme will be helpful in the production of L-fuculose with an efficient and simple method without producing any by-product.

Cold-active extracellular alkaline protease from an alkaliphilicStenotrophomonas maltophilia: production of enzyme and its industrial applications

2009 ◽  
Vol 55 (11) ◽  
pp. 1294-1301 ◽  
Author(s):  
Mohammed Kuddus ◽  
Pramod W. Ramteke
Keyword(s):  
High Efficiency ◽  
Western Himalaya ◽  
Industrial Applications ◽  
Culture Conditions ◽  
Maximum Activity ◽  
Exchange Chromatography ◽  
Protease Production ◽  
Cold Active ◽  
Metalloprotease Inhibitors ◽  
Potential Component

A novel psychro-tolerant bacterium Stenotrophomonas maltophilia (MTCC 7528) with an ability to produce extracellular, cold-active, alkaline, and detergent-stable protease was isolated from soil samples obtained from Gangotri glacier, Western Himalaya, India. The culture conditions for higher protease production were optimized with respect to incubation time, agitation, substrate, pH, and temperature. Maximum protease production of 56.2 U·mL–1was achieved in the medium at 20 °C and pH 9.0 after 120 h incubation. The protease was partially purified by ion-exchange chromatography and approximately 55-fold purification was achieved. The purified enzyme was a 75 kDa protease with maximum activity and stability at pH 10 and 20 °C. The activity of enzyme is stimulated by Mn2+and inhibited completely by metalloprotease inhibitors, indicating that it is a metalloprotease. The protease showed excellent stability and compatibility with commercial detergents and exhibited high efficiency for the removal of different types of protein-containing stains at low temperature. The wash performance analysis of blood and grass stains on cotton fabric showed an increase in reflectance by 26% and 23%, respectively, after treatment with enzyme in comparison to detergent only. These results indicate that it may be a potential component to use as a detergent additive for cold washing and in environmental bioremediation in cold regions.

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