Study of a new spectrophotometric end-point assay for lipase activity determination in aqueous media

Palacios, David; Busto, María D.; Ortega, Natividad

doi:10.1016/j.lwt.2013.10.027

Cited by 41 publications

(35 citation statements)

References 51 publications

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“…Several water‐soluble and water‐insoluble substrates are commonly used to assay lipase. Three of the most common substrates that have been used to assay cereal grain lipases are triacylglycerol (typically triolein or olive oil), p ‐nitrophenyl palmitate, and p ‐nitrophenyl butyrate (Prabhu et al 1999; Suzuki et al 2004; Wrolstad et al 2005; Palacios et al 2014). p ‐Nitrophenyl butyrate is a water‐soluble substrate and would therefore be expected to capture general esterase activity.…”

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confidence: 99%

Influence of Foliar Fungicide Treatment on Lipolytic Enzyme Activity of Whole Wheat

et al. 2017

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Lipolytic enzymes play a key role in the deterioration of whole wheat flour upon storage but may also be involved in plant disease and stress tolerance while the crop is in the field. Therefore, the purpose of this study was to determine the effect of foliar fungicide treatment on lipolytic activity in wheat. A significant cultivar × fungicide × year interaction for esterase (p‐nitrophenyl butyrate as substrate [EA‐B]) and lipoxygenase (LOX) activities was observed; however, a large portion of the variability was owing to year (environment). Fungicide influenced lipase (olive oil as substrate [LA‐O]), EA‐B, and LOX activities. Lipase (p‐nitrophenyl palmitate as substrate [LA‐P]) showed variation in terms of cultivar and year rather than the application of fungicide. Partial correlation (year as a partial variable) between LA‐P and EA‐B activities was observed (r = 0.78, P < 0.001), although neither was correlated with LA‐O. The influence of foliar fungicide on lipolytic enzyme activities depends mostly on growing conditions but is also affected by disease stress, disease resistance of the varieties tested, and the substrate being used in the assay.

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confidence: 99%

Influence of Foliar Fungicide Treatment on Lipolytic Enzyme Activity of Whole Wheat

et al. 2017

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“…Lipase activity was determined by the end-point test, using pNPpalmitate as a substrate according to the slightly modified procedure of Palacios et al [37]. The reaction mixture consisting 3.9 mL of 50 mM Tris-HCl buffer (pH 8) with gum arabic (1 g/L) and 1 mM pNP-palmitate was pre-warmed to 40°C whereupon crude enzyme extract was added (V = 0.1 mL).…”

Section: Lipase Assaymentioning

confidence: 99%

Proximate analysis of cold‐press oil cakes after biological treatment with Trametes versicolor and Humicola grisea

Budžaki

Strelec

Krnić

et al. 2018

Engineering in Life Sciences

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In order to increase the current knowledge on cold‐press oil cakes composition, the present study aims to determine the chemical composition of oil cakes from hull‐less pumpkin (Cucurbita pepo L.), flax (Linum usitatissimum L.), and hemp (Canabis sativa L.) before and after the biological treatment with Trametes versicolor and Humicola grisea using fungal‐based solid‐state technology. After 10 days of treatment, the content of ash, total nitrogen, total proteins, and total organic carbon increased in all the three oil cakes, while the content of ether extracts decreased. After treatment, the concentration of soluble carbohydrates decreased in pumpkin and hemp seed oil cakes, whereas it increased in flaxseed oil cake. During treatment with T. versicolor, the content of fructose significantly increased in hull‐less pumpkin seed oil cake. Fiber content decreased in pumpkin and flaxseed oil cakes after treatment with both of the fungi, whereas it increased in flaxseed oil cake.

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“…Oilseed lipases have attracted much interest because of their great potential for commercial exploitation as industrial enzymes, including those isolated from oilseed species that can be considered as underutilized (Enujiugha et al, 2004). These enzymes are effective catalysts of various inter-esterification and trans-esterification reactions (Gupta et al, 2004;Romdhane et al 2012) in the presence of decreasing amounts of water and often in the presence of organic solvents (Ogino et al, 2004;Palacios et al, 2014). Because of their versatility, lipases are the enzymes of choice for multiple applications in different fields: food, pharmaceutical, chemical, detergent, leather, textile, cosmetics and paper industries, for organic synthesis, biodiesel production or even environmental management (Pandey et al, 1999;Sharma et al, 2002;Barros et al, 2010;Foresti and Ferreira, 2010).…”

Section: Reverse Transcription (Rt)-pcrmentioning

confidence: 99%

Cloning, Sequence Analysis and Expression Patterns during Seed Germination of a Rapeseed (Brassica napus L.) G-x-S-x-G-motif Lipase Gene

Ghram

Belguith

Mustapha

et al. 2016

Not Bot Horti Agrobo

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Lipases catalyze the hydrolysis of ester bonds in triacylglycerides, generating glycerol and free fatty acids. These enzymes are encoded by extremely complex gene families, and appear to fulfil many different biological functions. Although they are present in all types of organisms, available information on plant lipases is still very limited, as compared to their bacterial and animal counterparts. A full-length clone, BnLIP, encoding a putative lipase, has been isolated by PCR amplification of Brassica napus genomic DNA, with oligonucleotide primers derived from the sequence of an Arabidopsis thaliana homologue. The clone included an open reading frame of 1581 bp encoding a polypeptide of 526 amino acids, with a calculated molecular mass of 59.5 kDa. Analysis of the deduced protein sequence, sequence alignment with homologous proteins from related plant species, and a phylogenetic analysis revealed that the BnLIP protein belongs to the 'classical' GxSxG-motif lipase family. RT-PCR assays indicated that the BnLIP gene is expressed specifically, but only transiently, during seed germination: the lipase mRNA was not present at detectable levels in ungerminated seeds, was detected only three days after seed imbibition, but its levels decreased rapidly afterwards. No expression was observed in roots, stems or leaves of adult plants. This expression pattern suggests that BnLIP is one of the lipases involved in the hydrolysis of triacylglycerides stored in rapeseed seeds, ultimately providing nutrients and energy to sustain seedling growth until photosynthesis is activated.

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Study of a new spectrophotometric end-point assay for lipase activity determination in aqueous media

Cited by 41 publications

References 51 publications

Influence of Foliar Fungicide Treatment on Lipolytic Enzyme Activity of Whole Wheat

Influence of Foliar Fungicide Treatment on Lipolytic Enzyme Activity of Whole Wheat

Proximate analysis of cold‐press oil cakes after biological treatment with Trametes versicolor and Humicola grisea

Cloning, Sequence Analysis and Expression Patterns during Seed Germination of a Rapeseed (Brassica napus L.) G-x-S-x-G-motif Lipase Gene

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