Pectin Identification Assay Kit

Reference code: K-PECID
SKU: 700004325

500 assays per kit

Content: 500 assays per kit
Shipping Temperature: Ambient
Storage Temperature: Short term stability: Ambient,
Long term stability: See individual component labels
Stability: > 2 years under recommended storage conditions
Analyte: Pectin
Assay Format: Spectrophotometer
Detection Method: Absorbance
Wavelength (nm): 235
Signal Response: Increase
Reaction Time (min): ~ 30 min
Application examples: Food ingredients (e.g. citrus fruit and apple) and other materials.

The Pectin Identification Assay Kit is suitable for the identification of pectin in food ingredients. This kit now employs a new pectate lyase from Aspergillus niger.

See the complete list of our polysaccharide assay kit products.

Scheme-K-PECID PECID Megazyme

Advantages
  • Very cost effective 
  • All reagents stable for > 2 years after preparation 
  • Only enzymatic kit available 
  • Simple format 
  • Standard included
Documents
Certificate of Analysis
Safety Data Sheet
FAQs Assay Protocol
Publications
Publication

Polysaccharide utilization loci from Bacteroidota encode CE15 enzymes with possible roles in cleaving pectin-lignin bonds.

Seveso, A., Mazurkewich, S., Banerjee, S., Poulsen, J. C. N., Lo Leggio, L. & Larsbrink, J. (2024). Applied and Environmental Microbiology, 90(1), e01768-23.

Lignocellulose is a renewable but complex material exhibiting high recalcitrance to enzymatic hydrolysis, which is attributed, in part, to the presence of covalent linkages between lignin and polysaccharides in the plant cell wall. Glucuronoyl esterases from carbohydrate esterase family 15 (CE15) have been proposed as an aid in reducing this recalcitrance by cleaving ester bonds found between lignin and glucuronoxylan. In the Bacteroidota phylum, some species organize genes related to carbohydrate metabolism in polysaccharide utilization loci (PULs) which encode all necessary proteins to bind, deconstruct, and respond to a target glycan. Bioinformatic analyses identified CE15 members in some PULs that appear to not target the expected glucuronoxylan. Here, five CE15 members from such PULs were investigated with the aim of gaining insights on their biological roles. The selected targets were characterized using glucuronoyl esterase model substrates and with a new synthetic molecule mimicking a putative ester linkage between pectin and lignin. The CE15 enzyme from Phocaeicola vulgatus was structurally determined by X-ray crystallography both with and without carbohydrate ligands with galacturonate binding in a distinct conformation than that of glucuronate. We further explored whether these CE15 enzymes could act akin to pectin methylesterases on pectin-rich biomass but did not find evidence to support the proposed activity. Based on the evidence gathered, the CE15 enzymes in the PULs expected to degrade pectin could be involved in cleavage of uronic acid esters in rhamnogalacturonans.

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Publication

A combination of commercial and traditional food-source-derived enzymatic treatment acts as a potential tool to produce functional yuzu (Citrus junos) powder.

Jeong, H., Das, P. R., Kim, H., Im, A. E., Lee, B. B., Yang, K. Y. & Nam, S. H. (2023). Food Chemistry: X, 20, 100918.

Enzymatic modifications have been applied in citrus to enhance their physicochemical and biological properties and reduce their bitterness. Notwithstanding, research on the combination of enzyme treatment of yuzu is lacking. In this study, yuzu was treated with a combination of isolated cellulase NY203, pectinase UF, and cellulase KN, and this enzymatic treatment was found to increase monosaccharide, naringenin, and hesperetin levels. In contrast, dietary fiber, cellulose, hemicellulose, lignin, and pectin levels were decreased. Moreover, the enzymes disintegrated the inner and outer surface structures and chemical bonding of yuzu, thus improving its solubility rate, water-holding capacity, oil-adsorption capacity, cholesterol-binding capacity, and water-swelling capacity. Furthermore, NY203 + UF + KN combination treatment reduced the bitterness of treated yuzu by 50 % compared with the control. Additionally, NY203 + UF + KN treatment yielded a 28 % decrease in lipid accumulation and two-fold higher lipolytic activity in 3T3L-1 adipocytes. These findings are potentially beneficial to the food/nutraceutical industries regarding functional yuzu powder production.

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Publication

Multi‐block analysis for the correlation of physico‐chemical and rheological data of 42 fruit pulps.

Stafussa, A. P., Rampazzo, V., Fernandes, R. R., Franco, A. T., Bona, E., Maciel, G. M. & Haminiuk, C. W. I. (2019). Journal of texture studies, 50(2), 114-123.

The common dimension (ComDim) chemometric method for multi‐block analysis and hierarchical cluster analysis (HCA) were used to evaluate the data obtained from the physico‐chemical and rheological characterization of 42 commercial fruit pulps. The physico‐chemical characteristics and the rheological behavior of the pulps were found to be considerably different. The Herschel-Bulkley equation was fit to the steady‐state flow curves of the fruit pulps, and it was found to appropriately describe the materials, which showed a wide range of yield stresses. The soluble solids content and the yield stress were the main factors responsible for the sample discrimination in the multivariate statistical analysis. The ComDim model indicates that these parameters may have a direct correlation. Namely, the soluble solids amount can influence the viscosity, as demonstrated by the similar scores of the samples in both common components, and this corroborated with the HCA analysis.

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Publication
Optimization of Xylanase Production from Fermentation of Water Hyacinth (Eichhornia crassipes) using Trichoderma species.

Udeh, C. B., Ameh, J. B., Ado, S. A. & Okoduwa, S. I. R. (2017). Journal of Biotechnology Research, 3(3), 15-24.

Background: In the present study, optimized cultural conditions for enhanced production of xylanase from local soil isolate of Trichoderma species, using water hyacinth as a substrate in submerged culture fermentation is presented. Method: The Megazyme assay method was used for endo 1, 4-β-xylanase using Azo-xylan (Birchwood). Results: A continuous increase in xylanase production was observed with increasing level of substrate concentration in the medium and highest production was obtained with water hyacinth at 6% w/v level. Maximum xylanase production was achieved with a pH 5.0, incubation temperature of 30°C and agitation rate of 150 rpm. The highest production was achieved on day five of fermentation at optimum parameters under study. Conclusion: The study showed that production of xylanase can be cost effective using water hyacinth and can be implored on large scale for industrial applications.

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Safety Information
Symbol : GHS07, GHS08
Signal Word : Warning
Hazard Statements : H319, H351
Precautionary Statements : P201, P202, P264, P280, P305+P351+P338, P308+P313
Safety Data Sheet
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