Pectinase Production Research Articles

Pharmamedia and pectinase production by Bacillus subtilis Mz-12P.

Bacterial isolates collected from the environment were screened for pectinolytic activity, and a strain with the highest activity was selected and identified as Bacillus subtilis Mz-12. The presence of pectin hydrolase, lyase, and esterase activities was confirmed. Pectinase was purified and characterized. Enzyme production was optimized with respect to temperature, pH, and growth medium. Enzyme stability and activity were characterized under different temperatures and pH values. The results showed that this strain was capable of producing high yields of pectinase in commercial medium (Pharmamedia) 24.6U/mL compared to other media. The purified pectinase of 22.3kDa produced was constitutive in nature. The isolated enzyme from this strain displayed a wide range of temperature and pH stability, with the optimal activity observed at pH 9.0 and 50°C. These results indicate that the B. subtilis Mz-12 strain is a favorable candidate for industrial enzyme production. The use of Pharmamedia is reported for first time for pectinase production.

Batch cultivation and optimization of pectinase production using Bacillus sp. (BIOSMNF02) through RSM-D-optimal quadratic model

Batch cultivation and optimization of pectinase production using Bacillus sp. (BIOSMNF02) through RSM-D-optimal quadratic model

Unlocking the potential of rhizobacteria in Moroccan vineyard soils: Biocontrol of grapevine trunk diseases and plant growth promotion

Rhizospheric bacteria isolated from the root system of Vitis vinifera plants in Morocco were evaluated for their activities against fungi associated with grapevine trunk diseases namely Diplodia mutila, Neoscytalidium dimidiatum, Trichothecium roseum, and Neopestalotiopsis vitis. Those pathogens cause grapevine decline and impede growth and are known as the greatest threat to production worldwide. Among a collection of 196 rhizobacteria, twenty-four isolates exhibited potential antifungal activity against all the tested fungal pathogens. Based on the partial 16S rDNA genes, different genera were identified namely Bacillus, Pseudomonas, Achromobacter, Ensifer, and Brucella. In particular, Bacillus halotolerans (JFM-64 and JMS-14), Pseudomonas koreensis (JRSK-45), and Ensifer adhaerens (JRSK-84) were found to be the most effective strains. Furthermore, the potential of bacterial isolates to promote plant growth was assessed. The funding revealed that of twenty-four antagonist rhizobacteria, seventeen displayed protease and chitinase production, while fifteen, thirteen, and twelve bacteria demonstrated the production of amylase, cellulase, and pectinase respectively. Furthermore, thirteen bacterial isolates produced hydrocyanic acid (HCN), sixteen isolates harbor the ability to solubilize tricalcium phosphate and seventeen were able to produce siderophores and indole acetic acid (IAA). The results of the current study showed that the most effective bacterial isolates could exhibit traits other than Plant Growth-Promoting Rhizobacteria (PGPR). Our results showed that the bacterization of B. napus seedlings with the selected bacteria improved plant growth when compared to untreated controls. Autoclaved grape wood assays were used to further confirm the in vitro results. The growth of Diplodia mutila, Neopestalotiopsis vitis, Neoscytalidium dimidiatum, and Trichothecium roseum was effectively reduced by rhizobacterial isolate Pseudomonas koreensis (JRSK-45) by 97.31, 97.14, 94.17, and 91.91%, respectively. This study highlights the potential of specific rhizobacteria as a promising approach to controlling fungal trunk pathogens associated with grapevine decline.

Screening of Rhizobacterial Isolates from Apple Rhizosphere for Their Biocontrol and Plant Growth Promotion Activity

Apple crops are prone to several diseases that limit their production—in particular, root rot caused by a new genus of oomycetes, mainly Phytopythium vexans. This study aims to screen antagonistic bacteria that can play an important role in the biological control of this pathogenic oomycete and to evaluate their capacity to promote plant growth. The dual culture test revealed that, out of 200 bacterial isolates, 16 have been able to inhibit the mycelial growth of P. vexans with inhibition rates greater than 50%. The selected isolates were identified based on the 16S rDNA genes: 14 bacteria belonging to the genus Bacillus, Stenotrophomonas, and the family Enterobacteriaceae. Notably, two isolates, B1 and M2-6 (identified as Bacillus velezensis), demonstrated the highest inhibition rates of 70% and 68%, respectively. These selected isolates were examined for their ability to produce different compounds related to biocontrol and plant growth promotion. Furthermore, the 16 selected isolates were evaluated for their ability to produce compounds associated with biocontrol and plant growth promotion, including hydrolytic enzymes (cellulases, proteases, and amylases), HCN (hydrogen cyanide) production, phosphate solubilization, IAA (indole-3-acetic acid) production, pectinase production, and stimulation of sorghum bicolor growth in vivo. Variations were observed among the bacterial isolates in terms of their compound production and phytostimulation capabilities. However, the secretion of proteases was consistently detected in all antagonistic isolates. The presence of genes responsible for the production of antifungal lipopeptides (bacillomycin, fengycin, and iturin) in the selected bacterial isolates was determined using polymerase chain reaction (PCR) techniques, while the absence of genes involved in surfactin biosynthesis was also confirmed through PCR studies. These isolates demonstrated inhibitory activity through the production of proteases and antifungal lipopeptides. Further research is needed to explore their potential use in biological control strategies and to improve apple crop productivity.

Isolation of Pectinolytic Bacteria from Decayed Orange Peel (Citrus sinensis) in Clarification of Tea Extract

Background: Production of microbial enzymes at the industrial scale and their commercialization has attained a lot of value and public focus. Usage of micro organisms as bio-reactors begins due to the evolution of enzymes produced by microorganisms. There are so many industrially significant enzymes are originated from microbes, that include pectinases, lipases, amylases, proteases, xylynases etc. Methods: The actual work involved the use of microbes isolated from the decaying orange peel and tomato pulp for the extraction of the pectinase enzyme. The organisms were isolated and screened from the samples and were cultured onto pectin agar plate. Morphological and microscopic identification revealed that the bacteria isolated was Bacillus sp. Pectinase production media was later used for the lab scale production of pectinase enzyme by inoculating the bacteria and incubating for 48 hours. The enzyme thus produced was purified by Various methods. The pectinase enzymes isolated from bacillus sp. were used for improvement of tea leaves quality and clarification. The enzymes were characterized and purified. Results: The outcome of both purified pectinase enzymes and crude enzyme preparation on the improvement of tea extracts were determined in terms of flavanoids (310mg/gm), DPPH (49mg/gm), caffeine content (0.56-0.95), moisture content (7.2-6.7%), ash (4.1-4.6%), total phenol content (285mg/gm), and pH(6) and the shelf life analysis of the tea produced. The results thus obtained can conclude that the use of Bacillus sp. in the industrial production of pectinase is highly beneficial. According to the findings obtained from the study the enzyme treated tea extract improves its various quality parameters than the tea extracts which is non enzyme treated. And the utilization of microbial pectinase produced from bio-waste were most cost effective and yield good results for industrial use.

The potential of in-house pectinolytic enzymes for industrial application

Pectinases are one of the essential groups of enzymes in the field of biotechnology and have applications in various industries including food, textile, paper industries, and waste management. Pectinases, like other industrial enzymes, are usually expensive. This research aimed at producing in-house pectinase from waste fruits, by an inductive mechanism. The study specifically optimized the production of in-house pectinases from mango and pawpaw peels used as substrates and also demonstrated the hydrolytic potential of the substrate-based in-house pectinase enzymes through viscosity analysis. The mango and pawpaw peels obtained from Blue Skies Co. Ltd. were oven-dried and milled to sieve particle sizes depending on the mode of the fermentation process. Measured amounts of the substrates were put into 50 ml Falcon tubes and subjected to both solid-state and submerged fermentation processes. The substrates were inoculated with one milliliter of Aspergillus niger isolate suspension and incubated at 30 °C for 2, 4, 6, 8, and 10 days under both fermentation processes. The crude enzyme extracts (in-house pectinolytic enzymes) obtained from the mango and pawpaw peels of both fermentation processes were used as enzyme sources for the hydrolysis of 1% w/v pectin solution prepared in phosphate buffer, pH 6.8 at 40 °C in viscosity analysis. The viscosities of the various treatments were recorded at different time intervals of 10, 20, and 30 min. Based on the viscosity analysis, it was observed that pectinolytic enzymes from pawpaw peels showed higher pectinolytic potential relative to the mango counterpart for both fermentation processes. However, there were consistent optima at day 4 for the mango peels and day 6 for the pawpaw peels using the submerged fermentation process. Also, there was a linear correlation between the pectinolytic activity and incubation period. The results obtained from this study show a higher potential to produce pectinases from agro-wastes such as mango and pawpaw peels for industrial purposes using an appropriate fermentation process.

ChsA, a Class Ⅱ Chitin Synthase, Contributes to Asexual Conidiation, Mycelial Morphology, Cell Wall Integrity, and the Production of Enzymes and Organic Acids in Aspergillus niger.

Chitin synthases (CHSs) are vital enzymes for the synthesis of chitin and play important and differential roles in fungal development, cell wall integrity, environmental adaptation, virulence, and metabolism in fungi. However, except for ChsC, a class III CHS, little is known about the functions of CHSs in Aspergillus niger, an important fungus that is widely applied in the fermentation industry and food processing, as well as a spoilage fungus of food and a human pathogen. This study showed the important functions of ChsA, a class II CHS, in A. niger using multi-phenotypic and transcriptional analyses under various conditions. The deletion of chsA led to severe defects in conidiation on different media and resulted in the formation of smaller and less compact pellets with less septa in hyphal cells during submerged fermentation. Compared with the WT, the ΔchsA mutants exhibited less chitin content, reduced growth under the stresses of cell wall-disturbing and oxidative agents, more released protoplasts, a thicker conidial wall, decreased production of amylases, pectinases, cellulases, and malic acid, and increased citric acid production. However, ΔchsA mutants displayed insignificant changes in their sensitivity to osmotic agents and infection ability on apple. These findings concurred with the alteration in the transcript levels and enzymatic activities of some phenotype-related genes. Conclusively, ChsA is important for cell wall integrity and mycelial morphology, and acts as a positive regulator of conidiation, cellular responses to oxidative stresses, and the production of malic acid and some enzymes, but negatively regulates the citric acid production in A. niger.

Utilization of wild Cressa cretica biomass for pectinase production from a halo-thermotolerant bacterium.

Halophytes are the native inhabitants of saline environment. Their biomass can be considered as a potential substrate for the production of microbial enzymes. This study was intended at feasible utilization of a halophytic biomass, Cressia cretica, for pectinase production using a halo- and thermo-tolerant bacterium, Bacillus vallismortis MH 10. The data from fractionation of the C. cretica biomass revealed presence of 17% pectin in this wild biomass. Seven different factors (temperature, agitation, pH, inoculum size, peptone concentration, substrate concentration and incubation time) affecting pectinase production using C. cretica were assessed through a statistical tool, Plackett-Burman design. Consequently, two significant factors (incubation time and peptone concentration) were optimized using the Central Composite design. The strain produced 20 IU mL-1 of pectinase after 24h under optimized conditions. The enzyme production kinetics data also confirmed that 24h is the most suitable cultivation period for pectinase production. Fourier transform infrared spectroscopy and scanning electron microscopy of C. cretica biomass ascertained utilization of pectin and structural changes after fermentation. The purification of pectinase by using DEAE column yielded specific activity and purification fold of 88.26 IU mg-1 and 3.2, respectively. The purified pectinase had a molecular weight of>65kDa. This study offers prospects of large-scale production of pectinase by halotolerant strain in the presence of economical and locally grown substrate that makes the enzyme valuable for various industrial operations. This article is protected by copyright. All rights reserved.

Screening and optimization of extracellular pectinase produced by Bacillus thuringiensis SH7

Abstract The objective of the current research was to identify and evaluate the possibility of production of pectinase, also known as pectin degrading enzymes, from indigenous bacterial strains. Qualitative screening of isolated bacterial strains showed that among 29 bacterial strains, 5 have maximum enzymatic activity. The highest pectinase producing strains were quantitatively analyzed for enzyme production. SH7 strain was found as highest pectinase producer (0.77 IU/mL) that was further analyzed to molecular level by amplification of 16s rRNA. It was found 100% similar with other reported strains of Bacillus thuringiensis. Medium optimization was performed to optimize fermentation conditions for maximum enzyme yield. An experimental design containing 12 experimental runs was designed by Plackett–Burman design (PBD). Maximum pectinase activity was obtained at 45°C after 24 h when the growth medium was supplemented with 2.5% nitrogen, 5.0% substrate, MgSO4 as metal ion, 1% inoculum size, and pH was adjusted to 6. Factorial regression analysis of the PBD design was performed and the overall design was also found significant in terms of R square value. In PBD, the most significant factors for production were temperature, pH, metal ion concentration, and nitrogen source. Central composite design (CCD) design consisting of 26 experimental runs was employed to optimize these four significant factors. The overall model summary showed maximum pectinase activity (19.2 IU/mL) at 37°C temperature, 0.08 NaCl, 1.7% nitrogen source, and pH 8.4. In CCD, NaCl, nitrogen source, and pH were also reported as significant factors by the Pareto chart, probability plots, and 3D interactions.

Enzymatic One-Pot Hydrolysis of Extracted Sugar Beet Press Pulp after Solid-State Fermentation with an Engineered Aspergillus niger Strain

Extracted sugar beet press pulp (SBPP) is a promising agricultural residue for saccharification and further bioconversion. Combining solid-state fermentation of SBPP with engineered Aspergillus niger for enzyme production followed by hydrolysis of additionally added SBPP in the same bioreactor was studied to produce a sugar solution (hydrolysate) in a one-pot process. The initial aerobic solid-state fermentations were carried out in duplicate on non-milled, wet SBPP (moisture content of 72% (w/v)) with an A. niger strain engineered for constitutive pectinase production for 96 h, and this resulted in polygalacturonase activities of up to 256 U mL−1 in the wet media. Afterwards, water was added to the bioreactor, and the remaining solids were suspended by stirring to dissolve the hydrolytic enzymes. Metabolic activities of A. niger were inactivated by a N2-atmosphere and by increasing the temperature to 50 °C. High solid loads of milled SBPP were added to the stirred-tank reactor with a delay of 24 h to enable sugar yield calculations based on the compositional analysis of the SBPP used. The resulting final sugar concentrations of the hydrolysate after 166 h were 17 g L−1 d-glucose, 18.8 g L−1 l-arabinose, and 12.5 g L−1 d-galacturonic acid, corresponding to sugar yields of 98% d-glucose, 86% l-arabinose, and 50% d-galacturonic acid, respectively. Including the other sugars released during enzymatic hydrolysis in the one-pot process (d-xylose, d-mannose, d-galactose), a total sugar concentration of 54.8 g L−1 was achieved in the hydrolysate. The one-pot process combining hydrolytic enzyme production in solid-state fermentation with high solid loads during enzymatic hydrolysis of the milled SBPP reduces hydrolytic process costs by replacing chemical pre-treatments, enabling the in situ production of SBPP-adapted hydrolytic enzymes, as well as avoiding intermediate enzyme extraction and preparation steps.

Potential Application of Suaeda fruticosa and Cressa cretica Biomass as a Substrate for Pectinase Production by Geotrichum candidum

Potential Application of Suaeda fruticosa and Cressa cretica Biomass as a Substrate for Pectinase Production by Geotrichum candidum

Production and Biochemical Characterization of Aspergillus japonicus Pectinase Using a Low-Cost Alternative Carbon Source for Application in the Clarification of Fruit Juices

Production and Biochemical Characterization of Aspergillus japonicus Pectinase Using a Low-Cost Alternative Carbon Source for Application in the Clarification of Fruit Juices

Pectinase production by fungal-based solid-state fermentation of selected agricultural wastes

Agricultural waste is the residues from growing and processing raw agricultural products. They can be properly managed using fungi to produce economical materials such as pectinase enzymes that act as biological agents which are applicable in many areas. This research was aimed at producing pectinase by fungal-based solid-state fermentation of agricultural wastes. Fungi were isolated from dump sites soil using the pour plate method. These fungal isolates were inoculated into the pretreated agricultural waste, including watermelon, mango, and pineapple peels. The degradation period was 15 days on mineral salt solid media using separate flasks for each waste and fungus. They were incubated at room temperature (28°C). The pectinase was assayed using pectin and DNSA (dinitrosalicyclic acid). Fungal isolates were identified and screened for pectinase production using standard methods. The pH and temperature were optimized to study the effect on pectinase activities using standard procedures and pectinase was purified using column sephadex G-100. Molecular identifications were carried out on the isolates using 18srRNA gene primers. The fungi were identified as Aspergillus niger strain AGF3 (OM273994), Penicillium Chrysogenum strain AGF2 (OM273982) and Cladosporium tenuissimum strain AGF1 (OM273981). Aspergillus niger strain AGF3 (OM273994) produced the highest specific pectinase activities in mango waste (2400 U/mg. protein/ mL and it can be compared to what was produced by Cladosporium tenuissimum strain AGF1 (OM273981) (1590 U/mg. protein/mL). High specific pecrtinase activity was also obtained from pineapple peels (2200 U/mg. protein/mL) produced by Cladosporium tenussimum strain AGF1 (OM273981). It can be concluded in this study that Aspergillus niger strain AGF3 (OM273994) and Cladosporium tenuissimum strain AGF1 (OM273981) were the best producers of pectinase using mango and pineapple peels, while Penicillium chrysogenum strain AGF2 (OM273982) produced substantial pectinase in all the three agricultural wastes but not at higher levels.

Optimization of the physicochemical parameters for production of pectinase by Aspergillus niger AG-1

Optimization of the physicochemical parameters for production of pectinase by Aspergillus niger AG-1

Assessment of cultivation parameters influencing pectinase production by Aspergillus niger LFP-1 in submerged fermentation

BackgroundPectinase is helpful in food and beverage industries, particularly in the preparation of fruit juice, the extraction of vegetable oil, and the fermentation of coffee. The current work aimed to screen Aspergillus niger LFP-1, a recently identified fungal strain, for its ability to produce pectinase and to ascertain the contribution of various physicochemical factors to pectinase production. ResultsThe primary and secondary pectinase activity screenings by Aspergillus niger LFP-1 were performed using pectin screening agar and shake flask system, respectively. The finding revealed that the locally isolated strain is able to secrete favourable pectinase production. Before improvement, the pectinase production was 0.88 ± 0.09 U/mL. However, the improved conditions such as 6 days of the cultivation period, agitation speed of 150 rpm, inoculum size of 1 × 106 spores/mL, 2.5% (w/v) citrus pectin, and 0.4% (w/v) ammonium nitrate could significantly increase pectinase production up to 7.41 ± 0.24 U/mL, representing an 88% increase. In this study, supplementing 2.5% (w/v) citrus pectin to the culture medium as a carbon source increased enzyme production by up to 3.07 ± 0.17 U/mL. Meanwhile, 0.4% (w/v) ammonium nitrate was used as a nitrogen source yielding the highest enzyme activity with a value of 6.86 ± 0.07 U/mL. ConclusionThus, the locally isolated fungal strain, A. niger LFP-1 has outstanding pectinase-producing capability and can be utilized for the commercial production of pectinase. The improved cultural conditions significantly increase pectinase production and shorten the incubation period from 8 days (before improvement) to 6 days (after improvement).

Pectinase Production from Saccharomyces Cerevisiae Using Orange Peels and Maize Cobs as Substrate for Solid-State Fermentation

Background of the Study: Degradation of wastes especially fruit waste is important because these wastes accumulate in the environment. The fruit wastes can be used to biosynthesize pectinase enzyme at a cheaper rate due its numerous industrial applications. The ability of Saccharomyces cerevisiae to degrade these wastes to produce pectinase enzyme was exploited.
 Aim: The aim of this study is to isolate and characterize Saccharomyces cerevisiae and study the optimal conditions needed for pectinase production on the orange peel with maize cobs and study the effectiveness of the enzymes produced in the extraction of orange juice.
 Place and Duration of Study: The study was conducted at the Microbiology Laboratory of Abubakar Tafawa Balewa University Bauchi, Bauchi State, Nigeria, between August to September 2021.
 Methodology: Soil samples from the orange seller stand was collected, serial dilution method was used to reduce the solution to a more usable concentration, and the samples were streaked on Yeast Peptone Dextrose Agar (YPDA). The plates were incubated for 3 to 9 days at 28+- oC. The isolated yeast was identified based on the morphological and biochemical test, the isolates were inoculated on the prepared fermentation media under different optimal conditions. The crude enzyme were extracted, and the extracts were tested for pectinase activity using the dinitrosalicylic reagent (DNS) method for the presence of reducing sugar. The resulting pectinase was determined to effectively extract juice from orange mash.
 Results: Saccharomyces cerevisiae showed relatively pectinase hydrolysis using orange peels and maize cobs as substrate by solid-state fermentation under predetermined optimum fermentation conditions. Optimization for the pectinase production was done by altering the conditions for the production medium. Pectinase activity of (2.81 + 2.31 ug/ml) was observed at 72hr of incubation at 35oC.
 Conclusion: The study demonstrates that orange peel and maize cob can be successfully used to induce the production of pectinase using Saccharomyces cerevisiae under solid-state fermentation.

Valorization of agro-industrial residues for pectinase production by Aspergillus aculeatus: Application in cashew fruit juice clarification

Valorization of agro-industrial residues for pectinase production by Aspergillus aculeatus: Application in cashew fruit juice clarification

A comparative study of Cellulomonas sp. and Bacillus sp. in utilizing lignocellulosic biomass as feedstocks for enzyme production

The demand for enzymes is increasing continuously due to their applications in various avenues. The pectin-hydrolyzing bacteria, Cellulomonas sp. and Bacillus sp., isolated from forest soil have the potential to produce industrially important enzymes (pectinase, PGase, Cellulase, and xylanase). However, these bacteria have different optimal cultural conditions for pectinase production. The optimal cultural conditions for Cellulomonas sp. were room temperature (25-26℃), pH 7, 1% inoculum volume, and 1.5% citrus pectin with 8.82 ± 0.92 U/mL pectinase activity. And Bacillus sp. illustrated the highest pectinase activity (12.35 ± 0.72 U/mL) at room temperature, pH 10, 1% inoculum volume, and 1.5% pectin concentration. Among the different agro-wastes, the orange peel was found to be the best substrate for pectinase, PGase, and cellulase activity whereas barley straw for xylanase activity. Further, Cellulomonas sp. and Bacillus sp. illustrated higher pectinase activity from commercial pectin compared to orange peel showing their preference for commercial citrus pectin. In addition, the optimization by the Box-Behnken design increased pectinase activity for Cellulomonas sp., while a noticeable increase in activity was not observed in Bacillus sp. Besides, all the agro-wastes exploited in this study can be used for pectinase, PGase, and xylanase production but not cellulase. The study revealed that each bacteria has its specific optimal conditions and there is a variation in the capacity of utilizing the various lignocellulosic biomass.

The interplay between (−)-epigallocatechin-3-gallate (EGCG) and Aspergillus niger RAF106, an EGCG-biotransforming fungus derived from Pu-erh tea

Although (−)-epigallocatechin-3-gallate (EGCG) exhibits various bioactivities, its low bioavailability and toxicity at high concentrations limit its application. Microbial biotransformation of EGCG could improve its bioavailability and bioactivities, but the interplay between EGCG and EGCG-transforming microbes was little known. Here, 50 g/L or less of EGCG was completely degraded at 48 h when co-incubated with Aspergillus niger RAF106 in potato dextrose broth. The degradation was accompanied by an unchanged radical-scavenging activity and increase in the production of (−)-epigallocatechin and gallic acid, which were degraded as the fermentation time increased. According to the compound structure, (−)-epicatechin and (−)-catechin were discovered after 120 h. When co-incubated with EGCG, RAF106 formed dispersed mycelia and grew faster. The inhibition of conidial agglomeration and changes in the ultrastructure of hyphal wall coincided with the inhibition of pellet formation. Additionally, the addition of EGCG increased the cellulase and pectinase activities and altered the transcripts of 1394 genes, including those associated with carbohydrate metabolism and fungal growth and development. Conclusively, co-incubation of EGCG and RAF106 resulted in EGCG conversion into smaller molecules, inhibition of fungal pellet formation, increased fungal growth and production of cellulases and pectinases, and significant changes in hyphal morphology and transcripts of several phenotype-related genes.

Isolation and Screening of Dye Degrading Lignocellulolytic Bacteria from Sundarban Mangrove Ecosystem, West Bengal, India

The present research work was carried out on isolating lignocellulolytic enzyme-producing natural bacterial isolates of the Sundarban Mangrove ecosystem in West Bengal, India. Multiple bacterial isolations and qualitative as well as quantitative screening of the isolates was conducted by selective media plates and dye decolorization assay. Growth characterization of the top three isolates, namely GD1, GD2, and GD3, was determined in both nutrient broth and selective media. GD1 showed laccase activity in ABTS plate and decolorized congo red, malachite green, and methylene blue by 64.82%, 47.69%, and 33.33%, respectively, which is the inherent property of laccase. Along with the maximum laccase activity (9.72U/L), it also showed a little amount of cellulase (5.8U/ml) and pectinase (0.55U/ml) activity in the enzyme assay. GD2 showed maximum cellulase activity (6.56U/ml) with only 3.3% degradation of congo red and 39.43% degradation of malachite green. Like GD1, GD2 also bears 5.6U/L laccase and 0.12U/ml pectinase enzyme activity. The last isolate, GD3 specialized in pectinase production and having 4.4U/ml enzyme activity, degraded congo red by 66.75% and malachite green by 54.26%.All isolates showed activity between 30° and 37°C, and pH ranges from 4.5 to 7. The outcomes of this research will be useful in the fiber industry like jute or banana, dye industry, pulp-paper industry, and textile industry for waste remediation, recycling, and fiber modification.