Name: Tributyrin Agar
Brand: Molecular Depot
SKU: B2017203
Price: 695 USD
Availability: InStock
Rating: 5 (2 reviews)

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Tributyrin Agar

Original price was: $1,395.00.Current price is: $695.00.

Catalog Number: B2017203 (500 g)
Tributyrin Agar is a high quality microbiological growth medium used primarily for the detection and differentiation of lipase-producing microorganisms. Lipases are enzymes that hydrolyze triglycerides, such as tributyrin, into glycerol and free fatty acids. Tributyrin Agar contains tributyrin as the primary lipid substrate, which makes it an ideal medium for observing lipolytic activity. This product has been used as a molecular tool for various biochemical applications. It has also been used in a wide array of other chemical and immunological applications. Custom bulk amounts of this product are available upon request.

Live enquiry about this product via Text/SMS: 1-858-900-3210.

In stock

SKU: B2017203 Categories: Media, Microbiology Tag: MD 1000

Product Description

Tributyrin Agar
Catalog number: B2017203
Lot number: Batch Dependent
Expiration Date: Batch dependent
Amount: 500 g
Molecular Weight or Concentration: N/A
Supplied as: Powder
Applications: a molecular tool for various biochemical applications
Storage: RT
Keywords: Tributyrin Agar
Grade: Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um.

References:
1: Riley TV. A note on hydrolysis of tributyrin by Branhamella and Neisseria J Appl Bacteriol. 1987 Jun;62(6):539-42.
2: Farooq S, Ganai SA, Ganai BA, Mohan S, Uqab B, Nazir R. Molecular characterization of lipase from a psychrotrophic bacterium Pseudomonas sp. CRBC14 Curr Genet. 2022 Apr;68(2):243-251.
3: Longhi R, Correia SS, Bruzaroski SR, Poli-Frederico RC, Fagnani R, Santana EHW. Pseudomonas fluorescens and Pseudomonas putida from refrigerated raw milk: genetic diversity and lipoproteolytic activity J Dairy Res. 2022 Feb 11:1-4.
4: Carrazco-Palafox J, Rivera-Chavira BE, Ramírez-Baca N, Manzanares-Papayanopoulos LI, Nevárez-Moorillón GV. Improved method for qualitative screening of lipolytic bacterial strains MethodsX. 2018 Feb 1;5:68-74.
5: Pirmanesh S, Kermanshahi RK, Gharavi S, Mobarak Qamsari E. Cloning, Expression, and Purification of a GDSL-like Lipase/Acylhydrolase from a Native Lipase-Producing Bacterium, Lactobacillus fermentum Iran Biomed J. 2022 Mar 1;26(2):153-9.
6: Jeon JH, Kim SJ, Lee HS, Cha SS, Lee JH, Yoon SH, Koo BS, Lee CM, Choi SH, Lee SH, Kang SG, Lee JH. Novel metagenome-derived carboxylesterase that hydrolyzes β-lactam antibiotics Appl Environ Microbiol. 2011 Nov;77(21):7830-6.
7: Sachan S, Iqbal MS, Singh A. Extracellular lipase from Pseudomonas aeruginosa JCM5962(T): Isolation, identification, and characterization Int Microbiol. 2018 Dec;21(4):197-205.
8: Hofmann K, Woller A, Huptas C, Wenning M, Scherer S, Doll EV. Pseudomonas cremoris sp. nov., a novel proteolytic species isolated from cream Int J Syst Evol Microbiol. 2021 Jan;71(1).
9: Fulton A, Hayes MR, Schwaneberg U, Pietruszka J, Jaeger KE. High-Throughput Screening Assays for Lipolytic Enzymes Methods Mol Biol. 2018;1685:209-231.
10: Distaso M, Cea-Rama I, Coscolín C, Chernikova TN, Tran H, Ferrer M, Sanz-Aparicio J, Golyshin PN. The Mobility of the Cap Domain Is Essential for the Substrate Promiscuity of a Family IV Esterase from Sorghum Rhizosphere Microbiome Appl Environ Microbiol. 2023 Jan 31;89(1):e0180722.

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