A Short Review on Various Screening Methods to Isolate Potential Lipase Producers: Lipases-the Present and Future Enzymes of Biotech Industry

Lanka, Suseela; Latha, J. Naveena Lavanya

doi:10.3923/ijbc.2015.207.219

Cited by 33 publications

(24 citation statements)

References 80 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%

“…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, ). Bornscheuer () explained that lipases can be differentiated from carboxyl esterases based on their substrate spectra: p ‐nitrophenyl palmitate ( p NPP) is hydrolyzed by lipases; p ‐nitrophenyl butyrate ( p NPB) is hydrolyzed by esterases.…”

Section: Discussionsupporting

confidence: 88%

Section: Lipid Substrate Bioassayssupporting

confidence: 87%

“…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, 2015;Tomulescu et al, 2015). Bornscheuer (2002) explained that lipases can be differentiated from carboxyl esterases based on their substrate spectra: p-nitrophenyl palmitate (pNPP) is hydrolyzed by lipases; p-nitrophenyl butyrate (pNPB) is hydrolyzed by esterases.…”

Section: Lipid Substrate Bioassaysmentioning

confidence: 99%

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Diversity, structure, and synteny of the cutinase gene of Colletotrichum species

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: Discussionsupporting

confidence: 88%

Section: Lipid Substrate Bioassayssupporting

confidence: 87%

Section: Lipid Substrate Bioassaysmentioning

confidence: 99%

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Diversity, structure, and synteny of the cutinase gene of Colletotrichum species

Villafana

Rampersad

2020

Ecology and Evolution

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“…Dada a grande especificidade, versatilidade e propriedades seletivas apresentadas pelas lipases estas enzimas estão se tornando cada vez mais significativas em várias aplicações industriais. Algumas das aplicações das enzimas lipolíticas podem ser vistas na área farmacêutica, na síntese de produtos químicos finos e de oleoquímicos, nas indústrias alimentícia, de couro, cosméticos, detergentes, no desenvolvimento de flavors, de fragrâncias, no pré-tratamento de águas residuais ricas em lipídios, na bioremediação de solos contaminados Research, Society and Development, v. 9, n. 4, e104942897, 2020 (CC BY 4.0) | ISSN 2525-3409 | DOI: http://dx.doi.org/10.33448/rsd-v9i4.2897 4 por óleos/gorduras e na síntese de biodiesel (Priji et al, 2016;Melani, Tambourgi e Silveira, 2019;Lanka & Latha, 2015;Ramos-Sánchez et al, 2015;Javed et al, 2018;Sharma, Sharma e Saxena, 2016).…”

Section: Introductionunclassified