Pectin Agar Research Articles

Characterization of yeast mutant strains for starter culture in Arabica coffee fermentation

Arabica coffee is the most popular and best-selling type of coffee. During coffee fermentation, microorganisms are essential for the production of metabolites and volatile compounds that affect coffee flavor quality. This work aimed to study the mutation, selection, and characterization of the Wickerhamomyces anomalus strain YWP1-3 as a starter culture to enhance the flavor quality of Arabica coffee. The results revealed that six mutants could produce relatively high levels of the pectinase enzyme on pectin agar media and exhibited high activity levels, ranging from 332.35 to 415.88 U/ml in mucilage broth. Strains UV22-2, UV22-3, UV41-1 and UV32-1 displayed higher levels of amylase activity than did the wild type. The UV22-2 and UV22-3 mutants exhibited the highest pectin degradation indices of 49.22% and 45.97%, respectively, and displayed significantly enhanced growth rates in nitrogen yeast base media supplemented with various sugars; thus, these mutants were evaluated for their ability to serve as a starter for fermentation of Arabica coffee. The cupping scores of coffees derived from UV22-2 and UV22-3 were 83.5 ± 1.5 and 82.0 ± 2.14, respectively. The volatile compounds in the roasted coffee fermented by UV22-2 were analyzed by GC‒MS, which revealed higher levels of furfuryl alcohol and furfuryl acetate than did the other samples. These findings suggested that UV22-2 could be an influential starter culture for Arabica coffee fermentation.

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.

Pectinase Production by Aspergillus Niger Ar-2 Using Orange Peels As Substrate

Pectinases are the group of enzymes that catalyzes the degradation of pectic substances. Pectinase are enzymes that are remarkably employed in most industries because they have a large variety of applications, such as increasing juice extraction by decreasing the viscosity of concentrates in cellulose fibre preparation, coffee/tea fermentation and also for the clarification of juices and wines. This research was carried out for pectinase production by Aspergillus niger AR2 using local orange peel as substrate. Aspergillus niger was isolated from spoiled orange fruit and identified using phenotypic and molecular techniques. The isolate was screened for pectinase production on pectin agar. Fermentation was carried out by Aspergillus niger AR2 at fermentation days 3, 4 and 5; the amount of substrate (15g), pH (5), temperature (300C) and inoculum density of 106 (spore/mL). After fermentation, crude pectinase was extracted for enzyme assay. Enzyme activity was measured based on the amount of D-galacturonic acid released by the crude enzyme. Pectinase produced was used for orange juice extraction from mashed oranges and compared with juice with no enzymes. The results have shown that maximum pectinase production by A. nigerAR2 was found to be at a temperature of 300C, inoculum density of 106 (spore/mL), pH 5 at day 5 using orange peels as substrate with an activity of 3.04±0.024 (U/ml). The result shows that the pectinase produced was effective in orange juice extraction from mashed oranges due to the increase in the volume of orange juice.

Antimicrobial Susceptibility of Clinical Isolates of Candida Species to Ethanolic Extracts of Ziziphus Abyssinica Leaves

Pectinases are the group of enzymes that catalyzes the degradation of pectic substances. Pectinase are enzymes that are remarkably employed in most industries because they have a large variety of applications, such as increasing juice extraction by decreasing the viscosity of concentrates in cellulose fibre preparation, coffee/tea fermentation and also for the clarification of juices and wines. This research was carried out for pectinase production by Aspergillus niger AR2 using local orange peel as substrate. Aspergillus niger was isolated from spoiled orange fruit and identified using phenotypic and molecular techniques. The isolate was screened for pectinase production on pectin agar. Fermentation was carried out by Aspergillus niger AR2 at fermentation days 3, 4 and 5; the amount of substrate (15g), pH (5), temperature (300C) and inoculum density of 106 (spore/mL). After fermentation, crude pectinase was extracted for enzyme assay. Enzyme activity was measured based on the amount of D-galacturonic acid released by the crude enzyme. Pectinase produced was used for orange juice extraction from mashed oranges and compared with juice with no enzymes. The results have shown that maximum pectinase production by A. nigerAR2 was found to be at a temperature of 300C, inoculum density of 106 (spore/mL), pH 5 at day 5 using orange peels as substrate with an activity of 3.04±0.024 (U/ml). The result shows that the pectinase produced was effective in orange juice extraction from mashed oranges due to the increase in the volume of orange juice.

SCREENING OF PECTINASE PRODUCING BACTERIA FROM SOIL AND PRODUCTION, PARTIAL PURIFICATION OF ENZYME

Bacterial pectinase enzyme is very much important at industrial level for different processes This present study focus on bacterial pectinase. Pectinase producing bacterial spp.is screen out from soil. About seven cultures of bacterial spp. were isolated from farmland soil sample using pectin agar plates. The selected isolates showed the zone of hydrolysis to confirmed the production of pectinase from the isolates. Among them the culture S4 showed prominent zone of hydrolysis surrounding the colony. Pectinase activity of each isolate were checked at an interval of 24 hrsusing DNSA method to access the enzyme efficiency produced by respective isolates. Keeping the ideal growth conditions the highest pectinase activity obtained among isolates was 11.43 U/ ml, by culture S4.Optimum condition for pectinase production was found at 72hrs. incubation period, 37˚C temperature and alkaline pH of 10 could be the optimum cultural conditions for bacterial strain S4. Bacterial strain S4 gave 40.85 U/ml partially purified enzyme.

Production and Optimization of Pectinase from Pectinolytic Fungi Cultivated on Mango peels and Pectin Subjected to Submerged Fermentation

Pectinases are the group of enzymes that degrade pectin. This study was conducted with the aim of isolation of efficient pectinase producing pectinolytic fungi from the decomposing mango peels using extracted mango peels pectin as a growth substrate under submerged fermentation, determining optimum pectinase production conditions with regards to some physicochemical parameters. The organisms were screened for the production of pectinase using Pectin agar media, and the two active pectinolytic fungi (P1 and P2) were isolated. pectinase production media was later used for the Lab scale production of pectinase by inoculating p1 and p2 and incubating for 7 days. The enzyme was extracted after seven days of fermentation and every day tested for their pectinolytic activity. P2 showed relatively higher pectinolytic activity and was therefore used for further studies. P2 was inoculated into a broth containing mango pectin under submerged fermentation. Results indicate that a pectin yield of mango peel 17.75%. Different parameters optimization processes were investigated on submerged fermentation namely pH, incubation period, temperature and substrate concentration optima were found 6, 4 days, 35oC and 1.5% respectively. The result suggests that mango peels have high pectin content and can be used for the value-added synthesis of pectinase.

Exploring the potential of engineering polygalacturonase-inhibiting protein as an ecological, friendly, and nontoxic pest control agent.

In plants, polygalacturonase-inhibiting proteins (PGIPs) play critical roles for resistance to fungal disease by inhibiting the pectin-depolymerizing activity of endopolygalacturonases (PGs), one type of enzyme secreted by pathogens that compromises plant cell walls and leaves the plant susceptible to disease. Here, the interactions between PGIPs from Phaseolus vulgaris (PvPGIP1 and PvPGIP2) and PGs from Aspergillus niger (AnPG2), Botrytis cinerea (BcPG1 and BcPG2), and Fusarium moniliforme (FmPG3) were reconstituted through a yeast two hybrid (Y2H) system to investigate the inhibition efficiency of various PvPGIP1 and 2 truncations and mutants. We found that tPvPGIP2_5-8, which contains LRR5 to LRR8 and is only one-third the size of the full length peptide, exhibits the same level of interactions with AnPG and BcPGs as the full length PvPGIP2 via Y2H. The inhibitory activities of tPvPGIP2_5-8 on the growth of A. niger and B. cinerea were then examined and confirmed on pectin agar. On pectin assays, application of both full length PvPGIP2 and tPvPGIP2_5-8 clearly slows down the growth of A. niger and B. cinerea. Investigation on the sequence-function relationships of PGIP utilizing a combination of site directed mutagenesis and a variety of peptide truncations suggests that LRR5 could have the most essential structural feature for the inhibitory activities, and may be a possible target for the future engineering of PGIP with enhanced activity. This study highlights the potential of plant-derived PGIPs as a candidate for future in planta evaluation as a pest control agent.

Carbon and Nitrogen Sources Effect on Pectinase Synthesis by Aspergillus niger Under Submerged Fermentation

Pectinases are the commercial enzymes that are abundantly employed in various industries like fruit juice industries for clarification, wine indutsry and paper industry for bleaching up pulp. The present work was done on culture conditions optimization for production of pectinases under submerged fermentation using wheat bran as a substrate. Fungal strains were isolated from vegetable waste dump yard soils of Warangal district of Telangana state and screened for their activity on pectin agar medium. Among 30 isolates, two fungal strains showed good activity and identified them as A. niger and A. flavus. The effects of the different carbon and nitrogen sources on pectinases viz. exo-PG, endo-PG, endo-PL and PME by A. niger with 1% wheat bran was carried out in submerged fermentation. These studies revealed that carbon and nitrogen sources have shown considerable influence on enzyme production. Among all the carbon sources tried, sucrose at 1% was shown to be efficient carbon source for all four types of pectinases under investigation. For endo-PG, endo-PL and PME maximum enzyme production were recorded on 8th day of incubation period but for exo-PG enhanced production was observed on 12th day. A. niger could not produce PME on 12th day from 2.50% to subsequent concentrations. Among nine different nitrogen sources were screened, maximum pectinase production was recorded in sodium nitrate at 0.2 % for A. niger. Endo-PG, endo-PL and PME maximum production were recorded on 8th day of incubation and for exo-PG maximum production was observed on 12th day. No PME production was observed in A. niger on 12th day.

Optimization of Pectinase and Protease Produced from Bacillus subtilis Isolated from Market Waste

Aims: The objective of the study was to produce and optimize protease and pectinase from Bacillus subtilis isolated from market waste.
 Place and Duration of Study: Department of Microbiology (laboratory unit), Michael Okpara University of Agriculture Umudike, Abia State Nigeria.
 Methodology: The production and optimization of protease and pectinase from bacteria isolated from solid market waste was investigated. Isolated bacteria from the waste were screened for protease and pectinase production using skim milk agar and pectin agar respectively. Using morphological, biochemical and molecular technique the enzymes producing isolate was confirmed as Bacillus subtilis. Protease and Pectinase were produced by Bacillus subtilis using submerged fermentation in gelatin broth and pectin broth respectively. The enzymes were purified using ammonium sulphate precipitation, dialysis and ion-exchange chromatography. Optimization using different temperatures, pH and nutrient sources was done. Enzyme activity was measured.
 Results: Purified protease exhibited maximum activity of 8.72U/ml at 40oC while pectinase exhibited maximum activity of 8.98U/ml at 50oC. Glucose as a carbon source and peptone as a nitrogen source gave optimum activity for both enzymes. Both pectinase and protease exhibited optimum activity at pH 9. There was significant difference (P=.05) in enzyme activity at different temperatures, pH and nitrogen sources for both protease and pectinase. There was no significant difference in pectinase activity at P=.05 for the different carbon sources while there was significant difference for protease activity for the different carbon sources at P=.05.
 Conclusion: Production of microbial enzymes such as protease and pectinase from waste material is an eco-friendly process and cheaper option for large scale use of enzymes in industry.

Production and characterization of extracellular pectinase from a newly isolated Bacillus species from fruit waste soil

The present investigation was carried for identification of pectinolytic bacteria and determination of their pectinolytic activity. The isolation was made from soil sample collected from fruit wastes. Screening of pectinolytic activity was achieved with pectin agar plate. Among 36 strains tested 12 shows pectinolytic activity. The potent isolate FWS II-4 was identified as Bacillus sp. and further used for enzyme production. Pectinase was produced by submerged fermentation and the purified. The purified enzyme demonstrated 3.40 mg/ml of total protein and 484.70 U/mg of specific activity. In characterization studies, the pectinase demonstrated good activity at pH 6.0 and 40 °C. Also, the bacterial strain showed maximum growth when the medium pH was 7.0 and incubated 37 °C.

Polygalacturonase production by Aspergillus nomius MR103 in solid state fermentation using Agro-industrial wastes

The present study was aimed at polygalacturonase production from Aspergillus nomius MR103 under solid state fermentation. A total of 57 fungal strains were obtained from mangrove soils collected from Gilakaladindi and Malakayalanka of Krishna District Andhra Pradesh. For the isolation of fungi these Soil samples were serially diluted and plated on pectin agar media plates. Among them, the isolate which showed maximum polygalacturonase activity was selected for this study. This strain was identified as A. nomius MR 103 by 18S rRNA sequences analysis. Pectin rich agro-industrial wastes like apple peel, citrus peel, orange peel, wheat bran, rice bran and sugarcane bagasse were used as substrates for polygalacturonase production by A. nomius MR 103. This strain was inoculated into the nutrient broth containing agro industrial wastes under solid state fermentation and amount of Polygalacturonase production was estimated. Maximum enzyme production of 4.83 IU/mg was recorded at pH 7.0 and temperature 35?C after 7 days of incubation, when orange peels were used as substrate. Addition of carbon and nitrogen sources to orange peel media improved the Polygalcturonase production. Sucrose as carbon and peptone as nitrogen sources were proved to be the best for maximum production of Polygalcturonase by A. nomius MR 103 on orange peel substrate. Utilization of agro-industrial by-products provided the establishment of a cost-efficient and sustainable process for enzyme production.

Isolation, Production and Application of Bacterial Pectinase for Industrial Use

Production of microbial enzymes at the industrial scale and their commercialization has gained a lot of focus and importance. Some of the industrially important enzymes from microbial origin include lipases, amylases, proteases, xylynases, pectinases etc. The objective of the study was production and application of bacterial pectinase for industrial use (clarification of fruit juices). Here the isolation of microorganism and characterization was done, then pectinase assay was performed and finally fruit juice was clarified using this enzyme. Here decayed orange peel was used as the sample and it was collected from a local market, South Kalamsseri- Cochin. The collected decayed orange part was subjected to serial dilution in order to isolate the organism. The dilutions were then plated on appropriate media (pecin agar media) and spread plate was performed. After the incubation time, colonies with zone were obtained which showed the production of pectinase enzyme. These isolated colonies were then inoculated to the petri plate containing pectin agar media and streak plate was performed. After 24 h incubation, the isolated colonies were subjected to Gram’s staining. It was Gram negative bacilli. The biochemical characterization (IMViC test) was done and VP Citrate tests were positive. Then the colonies were inoculated in Pectinase Production Broth. After 24 h incubation, the media was centrifuged for the isolation of enzymes. The enzyme assay was done by titration technique and the enzyme activity was found to be 0.78 U. This isolated enzyme was used for the clarification of apple juice and lime juice. According to the findings obtained from the study, the clarification of fruit juice by the use of bacterial pectinase is most cost effective and yield good results for industrial use.

Production of Pectinase from Bacillus sonorensis MPTD1.

Seven isolates from spoiled fruits and vegetables were screened for pectinase production using pectin agar plates and the most efficient bacterial strain, MPTD1, was identified as Bacillus sonorensis. Optimisation of various process parameters was done using Plackett-Burman and Box-Behnken designs and it was found that parameters like yeast extract, K2HPO4, incubation time, NaNO3 and KCl have a negative impact on pectinase production. Parameters like pH and MgSO4 and pectin mass fractions have a positive impact on pectinase production. The maximum obtained enzyme activity was 2.43 (μM/mL)/min. This is the first report on pectinase production by Bacillus sonorensis.

Characterisation of Growth Variability and Mycelial Compatibility of Botrytis Cinerea Isolates Originated from Apple and Strawberry in Lithuania

Abstract Botrytis cinerea Pers.:Fr. is a widespread necrotrophic pathogen causing grey mould on many economically important horticultural crops. The variability in various B. cinerea populations is known to be very high. Despite the economic importance, the variability of B. cinerea has not been investigated previously on fruit crops in Lithuania. The aim of the study was to characterise the variability of B. cinerea strains isolated from strawberry and apple in different growth conditions on various agar media and to assess mycelial compatibility among the isolates. Larger colony diameter after four days of incubation was observed for isolates from strawberry on potato dextrose and beer universal agars in 24 h dark or light regime, followed by pectin agar in 24 h light. Similarly, the maximum radial growth of the isolates from apple was on potato dextrose agar (dark), followed by beer universal agar (dark and light), after four days of incubation at 20 °C. In the mycelial compatibility tests, barrage formation was evident in mycelial contacts between several isolates, indicating their vegetative incompatibility. The tests revealed that 76% were compatible and 24% were incompatible among investigated strains.

Pectinolytic Activity of Mutagenic Strain of Leuconostoc Mesenteroides Isolated From Orange and Banana Fruit Waste

The aim of this study was to isolate pectinolytic bacteria from fermented banana and orange peels. The bacterial isolates were identified using standard biochemical method. The bacteria isolates were screened on pectin agar plates. All the isolates showed pectinolytic activity in terms of making zone surrounding their colony on pectin agar medium. Pectinase activity was determined by dinitrosalicylic (DNS) acid method while protein concentration in the fermentation broth was quantified by Lowry method. The screened isolate designated OP6 tentatively identified as Leuconostoc mesenteroides with highest pectinase activity was subjected to mutagen (Ethidium bromide). The mutants of Leuconostoc mesenteroides generated were screened for pectinase production in comparison with the parent (wild) type in submerged state fermentation. All the mutant strains generated from Leuconostoc mesenteroides had their pectinolytic activities repressed in comparison with the wild strain. Out of mutants screened, mutant designated AB4 have the highest pectinolytic activity 1.54 U/mg. The pectinase activity produced by AB4 was approximately 32% lower than the wild strain. The pretreatment of Leuconostoc mesenteroides with Ethidium bromide caused enzyme repression. The appreciable yield in pectinase activity displayed by the mutant strains when compared with the wild type suggests its industrial relevance. Therefore, use of other chemical mutagens can be tested for further strains improvement.

Morphological and molecular based identification of pectinase producing Bacillus licheniformis from rotten vegetable.

Pectinase catalyzed the degradation of pectin substances and has been used in various biotechnological industries. In the current study, 23 bacterial strains were isolated from rotten vegetables, soil and air. The isolated bacterial strains were qualitatively screened for pectinase production on pectin agar medium and only three strains HR 4, HR 21 and HR 23 were observed to produce extracellular pectinase. These strains were further screened quantitatively for pectinase production through submerged fermentation technology in pectin containing fermentation medium. Strain HR 4 from rotten brinjal (Solanum melongena) was found to produce higher pectinase as compared to others. The maximum pectinase producing bacterial strain was identified as Bacillus licheniformis on the basis of morphological, physiological and biochemical characteristics. For further confirmation of identification, 16S rDNA sequence analysis was performed. The 16S rDNA sequences were aligned and the phylogenetic tree was constructed. The phylogenetic tree confirmed that the strain was belonging to B. licheniformis. The 16S rDNA sequences of this new strain were submitted to GenBank and designated as B. licheniformis KIBGE-IB21 with the GenBank accession number JQ 411812. The newly isolated pectinase producing B. licheniformis used apple pectin as carbon and yeast extract as nitrogen source for maximum pectinase production.

Characterization of pectin depolymerising exo polygalacturonase by Bacillus sp. HD2 isolated from the gut of Apis mellifera L.

Background: Polygalacturonase is an important pectin degrading enzyme. The western honey bee (Apis mellifera L.) collects pollens from different flowers which are rich source of pectin. The microbiota in the gut of honey bee, release polygalacturonase enzyme and help in pectin digestion. This study aims to isolate and characterize novel polygalacturonase producing bacterial strain from honey bee’s gut. Methods: The bacterial strain was isolated by using pectin agar plate assay. The bacterial strain was identified on the basis of morphology and 16S rDNA sequence analysis. The enzyme assay was performed by using pectin as a substrate. Biomass of different fruits/vegetables was also used as a source of carbon during fermentation. The protein gel was run using SDS-PAGE for molecular weight determination of the polygalacturonase. Results: The bacterial strain showed the maximum growth, protein and polygalacturonase production at 72 hours of incubation. This bacterial strain was identified as new Bacillus sp. HD2. The sequence of this strain was successfully uploaded in NCBI Genbank database (Accession no. KP676929). The exo polygalacturonase produced by this strain of Bacillus was optimal at 40°C and exhibited enzyme activity in a wide range of pH from pH 5-12. The polygalacturonase production was enhanced by using yeast extract (3%) in the production medium and the enzyme activity was stimulated by Ca 2+ (2 mM) and SDS (200 mM). Biomass of apple’s peel (1%) was found as an excellent source of carbon for the polygalacturonase production in fermentation medium (17.11±0.46 μmol ml -1 min -1 ). In SDS-PAGE gel, the two clear bands of polygalacturonase were found at ~36 kDa and ~72 kDa. Conclusions: A new bacterial strain Bacillus sp. HD2 was isolated from the gut of honey bee. This strain produced the exo polygalacturonase enzyme. This enzyme was characterized under different pH and temperature and found to have maximum activity in pH 11 at 40°C. Apple peel’s biomass was found as a good source of carbon during fermentation for polygalacturonase production. The SDS-PAGE analysis confirmed two bands of protein with polygalacturonase activity at ~36 kDa and ~72 kDa.

Analysis of the Structural and Mechanical Properties and Micromorphological Features of Polymeric Films Based on Hydrocolloids of Vegetable Origin Used for the Production of Biodegradable Polymers

Modern research and technology approaches to the production of biodegradable polymeric materials based on renewable resources have been reviewed. It has been found that films prepared of cellulose, chitosan, gelatin, polypeptides, casein, soy, wheat, corn, rice, and maize are being commonly used at present. The structural and mechanical properties and micromorphological features of hydrocolloids of vegetable origin promising for the production of biodegradable polymers—starches, pectins, carrageenans, and agar—have been studied. It has been determined that, with respect to strength and suitability for use in films of individual components, all the studied hydrocolloids can be arranged in ascending order as follows: starches, carrageenans, pectins, agar. According to analysis of the structural and mechanical properties of the films, it has been shown that the best parameters are found for the samples based on pectin P1 and agar A2. The breaking stress for these materials is 52 and 77 MPa, respectively. The breaking strain is 11.5 and 8.0%, respectively. Analysis of the micromorphology has revealed the formation of surface microdiscontinuities in the films based on high methoxyl pectins P1 and P4 and unmodified corn starch S3 and the formation of wavy folds in the case of the films of kappa-carrageenan C1; these folds are formed during drying and decrease the tensile strength of the respective films. The found features will be used in the development of technologies for the production of biodegradable polymeric materials based on hydrocolloids of vegetable origin with enhanced performance and processing characteristics.

Screening of Cellulase and Pectinase by Using <i>Pseudomonas fluorescence</i> and <i>Bacillus subtilis</i>

A study was conducted to determine the Production of cellulase and pectinase enzyme by using Plant growth promoting rhizobacteria like Pseudomonas fluorescence and Bacillus subtilis. These to micro organism are isolated by serial dilution method. One gram of soil sample was diluted in to 10 ml of sterile distilled water and 1 ml of sample solution was serially diluted in 9ml of sterile water up to 10 dilution. Each sample from dilution 10-5 and 10-6 were taken and streaked in to KB and NA medium and incubate at 24 hrs. After 24 hrs Pseudomonas fluorescence and Bacillus subtilis was observed in the medium of KB and NA medium. Both the culture was sub cultured and maintain in the same for the further work. CMCase medium was prepared and sterilized by autoclave for 121 °C for 15 minutes after sterilization these medium contain petriplate was streaked by bacteria and incubates for 48h after incubation period a clear halo zone was produced by these bacteria among these bacteria Pseudomonas fluorescence are able to produce high amount of cellulose compare to Bacillussubtilis. Pectin agar medium was prepared and sterilized by autoclave for 121 °C for 15 minutes after sterilization these medium contain petriplate was streaked by bacteria incubates for 48h after incubation period a clear halo zone was produced by these bacteria, among these bacteria Pseudomonas fluorescence are able to produce high amount of Pectinase compare to Bacillus subtilis. Plant growth promoting rhizobacteria (PGPR) are beneficial bacteria that colonize plant roots and enhance plant growth by a wide variety of mechanisms.

Screening of Cellulase and Pectinase by Using <i>Pseudomonas fluorescence</i> and <i>Bacillus subtilis</i>

A study was conducted to determine the Production of cellulase and pectinase enzyme by using Plant growth promoting rhizobacteria like Pseudomonas fluorescence and Bacillus subtilis. These to micro organism are isolated by serial dilution method. One gram of soil sample was diluted in to 10 ml of sterile distilled water and 1 ml of sample solution was serially diluted in 9ml of sterile water up to 10 dilution. Each sample from dilution 10-5 and 10-6 were taken and streaked in to KB and NA medium and incubate at 24 hrs. After 24 hrs Pseudomonas fluorescence and Bacillus subtilis was observed in the medium of KB and NA medium. Both the culture was sub cultured and maintain in the same for the further work. CMCase medium was prepared and sterilized by autoclave for 121 °C for 15 minutes after sterilization these medium contain petriplate was streaked by bacteria and incubates for 48h after incubation period a clear halo zone was produced by these bacteria among these bacteria Pseudomonas fluorescence are able to produce high amount of cellulose compare to Bacillussubtilis. Pectin agar medium was prepared and sterilized by autoclave for 121 °C for 15 minutes after sterilization these medium contain petriplate was streaked by bacteria incubates for 48h after incubation period a clear halo zone was produced by these bacteria, among these bacteria Pseudomonas fluorescence are able to produce high amount of Pectinase compare to Bacillus subtilis. Plant growth promoting rhizobacteria (PGPR) are beneficial bacteria that colonize plant roots and enhance plant growth by a wide variety of mechanisms.