Isolation, Screening and Identification of Lipase Producing Fungi from Oil Contaminated Soil of Shani Mandir Ujjain

Wadia, Toshi; Jain, Shubha

doi:10.20546/ijcmas.2017.607.223

Cited by 19 publications

(13 citation statements)

References 5 publications

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“…Bioassays confirmed the ability of C. truncatum and C. brevisporum to produce and secrete cutinase enzyme in lipid substrate media. Growth characteristics for the identification of secreted lipase activity using Tween‐20, Rhodamine, and tributyrin agar plates were congruent with the results obtained from other studies (Lanka & Latha, ; Ramnath, Sithole, & Govinden, ; Wadia & Jain, ). As both Tween‐20 and Tributyrin can test positive with esterases, the positive fluorescence with Rhodamine B was used as the determining factor for the presence of lipase activity (Lanka & Latha, ; Tomulescu et al, ).…”

Section: Discussionsupporting

confidence: 88%

Section: Lipid Substrate Bioassayssupporting

confidence: 88%

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Diversity, structure, and synteny of the cutinase gene ofColletotrichumspecies

Villafana

Rampersad

2020

Ecology and Evolution

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Colletotrichum species complexes are among the top 10 economically important fungal plant pathogens worldwide because they can infect climacteric and nonclimacteric fruit at the pre and/or postharvest stages. C. truncatum is the major pathogen responsible for anthracnose of green and red bell pepper fruit worldwide. C. brevisporum was recently reported to be a minor pathogen of red bell pepper fruit in Trinidad, but has recently been reported as pathogenic to other host species in other countries. The ability of these phytopathogens to produce and secrete cutinase is required for dismantling the cuticle of the host plant and, therefore, crucial to the necrotrophic phase of their infection strategy. In vitro bioassays using different lipid substrates confirmed the ability of C. truncatum and C. brevisporum isolates from green and red bell peppers to secrete cutinase. The diversity, structure and organization and synteny of the cutinase gene were determined among different Colletotrichum species. Cluster analysis indicated a low level of nucleotide variation among C. truncatum sequences. Nucleotide sequences of C. brevisporum were more related to C. truncatum cutinase nucleotide sequences than to C. gloeosporioides. Cluster patterns coincided with haplotype and there was evidence of significant positive selection with no recombination signatures. The structure of the cutinase gene included two exons with one intervening intron and, therefore, one splice variant. Although amino acid sequences were highly conserved among C. truncatum isolates, diversity “hot spots” were revealed when the 66‐amino acid coding region of 200 fungal species was compared. Twenty cutinase orthologues were detected among different fungal species, whose common ancestor is Pezizomycotina and it is purported that these orthologues arose through a single gene duplication event prior to speciation. The cutinase domain was retained both in structure and arrangement among 34 different Colletotrichum species. The order of aligned genomic blocks between species and the arrangement of flanking protein domains were also conserved and shared for those domains immediately located at the N‐ and C‐terminus of the cutinase domain. Among these were an RNA recognition motif, translation elongation factor, signal peptide, pentatricopeptide repeat, and Hsp70 family of chaperone proteins, all of which support the expression of the cutinase gene. The findings of this study are important to understanding the evolution of the cutinase gene in C. truncatum as a key component of the biotrophic–necrotrophic switch which may be useful in developing gene‐targeting strategies to decrease the pathogenic potential of Colletotrichum species.

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Section: Discussionsupporting

confidence: 88%

Section: Lipid Substrate Bioassayssupporting

confidence: 88%

Diversity, structure, and synteny of the cutinase gene ofColletotrichumspecies

Villafana

Rampersad

2020

Ecology and Evolution

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“…Fungi are good sources of enzymes and reports from previous literatures have it that soils contaminated with oil often retain microbial diversity [15]. Out of the 9 fungi isolated from the vegetable oil contaminated soil following incubation on SDA, 5 isolates exhibited different magnitudes of zones of clearance when 3 % olive was used as a substrate (Table 2).…”

Section: Resultsmentioning

confidence: 97%

Characterization of Lipases from a Vegetable Oil Contaminated Soil Fungal Isolates

Emmanuel¹,

Labaran²,

Evans³

et al. 2020

ujmr

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Lipases are enzymes that hydrolyse lipids to produce free fatty acids and glycerol. Fungi were cultured on sabouraud dextrose agar (SDA) plates and identified using microscopic techniques. Screening for lipase producers was carried out on SDA media supplemented with 3 % olive oil at ambient temperature. M. pusillus, M. canis, A. fumigatus, Yeast and T. mentagrophytes were found to produce lipases in different amounts with Yeast and M. canis being the highest producers, they were further characterised for this reason. Lipase production was carried out using submerged fermentation. Both Yeast and M. canis produced lipases maximally at 72 h. Optimum pH and temperature of activity for the lipases from Yeast were determined to be 5 and 35 o C respectively whereas, those from M. canis were 6 and 40 o C correspondingly. Yeast and M. canis lipases had preference for olive oil than vegetable and palm oils and both enzymes were activated by K + , Mg 2+ and Ca 2+ and inhibited by Fe 3+ , Hg 2+ and Co 2+. The lipase enzyme from Yeast had V max of 0.0006 U/mL/Sec, K m of 0.4242 mM and K cat of 0.0004 S-1 while that from M.

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“…1) was obtained from the Department of Bioscience and Biotechnology, Banasthali Vidyapith which was previously isolated from the petrol pump soil sample of Newai Town (Raj) and screened for lipolytic activity on tributyrin agar (TBA) plates. It was subcultured & maintained on PDA slants and used for culture conditions optimization under submerged fermentation (SmF) (17).…”

Section: Isolation and Maintenance Of Lipolytic Fungimentioning

confidence: 99%

Optimization of culture conditions for extracellular fungal lipase production by submerged fermentation process

Shreya

Sharma

et al. 2018

Plant Sci. Today

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The present study aimed to optimize culture conditions for optimal growth and production of extracellular lipase. Lipolytic fungal strain named as S3St2 previously isolated from a petrol pump soil sample of Newai Town was used for optimization study. Among the tested carbohydrate carbon sources, polysaccharide-starch exhibited maximum lipase production (21.25±0.70 IU/ml/min) with highest specific activity (1.47±0.06 U/mg). Lipase activity and specific activity were higher with mustard oil 1 % (v/v) among all lipidic carbon sources. Among inorganic nitrogen source, potassium nitrate was found best inducer of lipase activity, malt extract supported the fungus growth (dry weight of cell pellets was 0.467 g) and exhibited maximum lipase activity among all organic nitrogen sources. Lipase activity was optimum at pH 8.0, indicates alkalophillic nature of production media supports the growth of fungus. Higher lipase activity (27.92±0.87 IU/ml/min) was detected at 28ºC. The incubation time of 5 days was found optimum for maximum lipase production (31.51±0.21 IU/ml/min). Keywords

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Isolation, Screening and Identification of Lipase Producing Fungi from Oil Contaminated Soil of Shani Mandir Ujjain

Cited by 19 publications

References 5 publications

Diversity, structure, and synteny of the cutinase gene ofColletotrichumspecies

Diversity, structure, and synteny of the cutinase gene ofColletotrichumspecies

Characterization of Lipases from a Vegetable Oil Contaminated Soil Fungal Isolates

Optimization of culture conditions for extracellular fungal lipase production by submerged fermentation process

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