Tryptone

Manufactured by ITW Reagents

Sourced in Spain

Tryptone is a complex mixture of peptides and amino acids derived from the enzymatic digestion of casein. It is a commonly used nutrient source in microbiology and cell culture applications, providing a rich source of nitrogen, carbon, and other essential growth factors for the cultivation of a variety of microorganisms.

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Lab products found in correlation

Yeast extract, by ITW Reagents (4 mentions) Lactose, by ITW Reagents (2 mentions) Xylan, by Merck Group (2 mentions) Laminarin, by Merck Group (2 mentions) D glucosamine, by Merck Group (2 mentions) Cm sepharose fast flow, by GE Healthcare (2 mentions) Sodium salt of carboxymethylcellulose, by Merck Group (2 mentions) Azokazein, by Merck Group (2 mentions) P nitrophenyl n acetyl β d glucosaminide p np glcnac p nitrophenyl n n diacetyl β d chitobioside p np glcnac 2 p nitrophenol, by Merck Group (2 mentions) N acetyl β d glucosamine, by Merck Group (2 mentions) Yeast extract, by Solabia (1 mentions) Tryptone, by Solabia (1 mentions) Potassium nitrate, by Avantor (1 mentions) Anaerocult a system, by Merck Group (1 mentions) Sodium, by Merck Group (1 mentions) Disodium hydrogen phosphate, by ITW Reagents (1 mentions) Potassium dihydrogen phosphate, by ITW Reagents (1 mentions) Glucose, by ITW Reagents (1 mentions) Glycerol, by ITW Reagents (1 mentions) Bis acrylamide, by Bio-Rad (1 mentions)

4 protocols using tryptone

Lactose Fermentation and Nitrate Reduction Assays

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Two concentrations of lactose and potassium nitrate were tested for a pool of strains in preliminary tests.
lactose fermentation was tested in a modified API 50CH medium containing the following: lactose 5 or 20 g.L⁻¹ (Panreac, Lyon, France), tryptone 10 g.L⁻¹, yeast extract 5 g.L⁻¹, K₂HPO₄, 0.25 g.L⁻¹, MnSO₄ 0.05 g.L⁻¹, and bromocresol purple 0.17 g.L⁻¹. The medium was inoculated using 1% (v/v) of 48-h cultures in YEL, and incubated at 30 °C under anaerobiosis (using the Anaerocult A system, Merck, Darmstadt, Germany). The production of acid from lactose was determined from the colour change of bromocresol purple from purple to yellow after 2, 5, and 7 days of incubation.
Nitrate reductase activity was detected by means of the Griess reagent (Biomérieux, Marcy l'Etoile, France) after incubation of cultures at 30 °C under microaerophilic conditions (air atmosphere without agitation) in a broth containing potassium nitrate, 0.5 or 1.5 g.L⁻¹ (VWR International, Fontenay-sous-Bois, France), tryptone (Biokar Diagnostics, Allone, France) 10 g.L⁻¹, yeast extract (Biokar Diagnostics) 5 g.L⁻¹, and glucose (Grosseron, Saint-Herblain, France) 1 g.L⁻¹, according to Dalmasso et al. (2011 (link)). The results of the tests were read after 2 and 5 days of incubation.
All the tests were carried out in triplicate.

de Freitas R., Madec M.N., Chuat V., Maillard M.B., Mukdsi M.C., Falentin H., de Carvalho A.F., Valence F, & Thierry A. (2015). New insights about phenotypic heterogeneity within Propionibacterium freudenreichii argue against its division into subspecies. Dairy Science & Technology, 95(4), 465-477.

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Recombinant Lipase LipA PSA01 Production

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Accurel MP1004, a porous polypropylene homopolymer powder with a particle size lesser than 0.4 mm, was purchased from Membrana GmbH (Obenburg, Germany). We purchased p-nitrophenyl palmitate (pNPP) and oleic acid (95%) from Sigma Aldrich (St Louis, Mo, USA). Tripalmitin was acquired from Spectrum Chemicals Mfg. Corp. (Gardena, CA, USA), and the coconut and Spanish extra virgin olive oils were bought from a local market. The reagents Bradford dye, acrylamide, and bisacrylamide were purchased from Biorad (Richmond, CA, USA).
We used the autoinducing medium for growth and expression of the recombinant lipase LipA PSA01: tryptone, yeast extract, lactose, glucose, glycerol, lactose, potassium dihydrogen phosphate, di sodium hydrogen phosphate, ammonium chloride, and magnesium sulfate were purchased from PanReac AppliChem (Barcelona, Spain). All solvents (hexane, ethanol, acetone, 2-propanol, ethyl acetate, and methanol) were acquired from JT Baker (Phillipsburg, NJ, USA). Gas chromatography standards and other chemicals used in this study (sodium, sodium hydroxide, TRIS, acetic acid, HEPES) were analytical reagents obtained from Sigma Aldrich (St Louis, Mo, USA).

Pulido I.Y., Prieto E, & Jimenez-Junca C. (2021). Ethanol as additive enhance the performance of immobilized lipase LipA from Pseudomonas aeruginosa on polypropylene support. Biotechnology Reports, 31, e00659.

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Chitosan and Chitin Preparation Protocol

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The chitosan (Mw ~ 370 kDa, DD 85%) and partially N-acetylated chitosan (Mw ~ 200 kDa, DD ~ 50%) were obtained from the Laboratory of Biopolymer Engineering of Institute of Bioengineering of Federal Research Center "Fundamentals of Biotechnology" of Russian Academy of Sciences (Moscow, Russia). Flake crab shell chitin was provided by BioProgress Co. (Shchelkovo, Russia) and grinded in laboratory mill. Colloidal chitin was prepared from powdered crab shell chitin by modi ed method of Rodriguez-Kabana et al. (1983) . Colloidal chitosan was prepared using the modi ed procedure (Helistö et al. 2001 (link)). N-acetyl-β-D-glucosamine, D-glucosamine, p-nitrophenyl-N-acetyl-β-D-glucosaminide (p-NP-GlcNAc), p-nitrophenyl-N,N'-diacetyl-β-D-chitobioside (p-NP-GlcNAc 2 ), p-nitrophenol, sodium salt of carboxymethylcellulose, azokazein, laminarin and xylan from birch were purchased from Sigma Chemical Co., USA. CM-Sepharose Fast Flow was purchased from GE Healthcare (USA). The nutritional components of culture media (tryptone, yeast extract etc.) were obtained from Panreac (Barcelona, Spain) and HiMedia Laboratories Pvt. Ltd. (Mumbai, India). All other reagents, including components for SDS-PAGE, TLC, buffer salts etc. used in the study were quali ed as analytical and high grade.

Aktuganov G.E., Safina V.R., Galimzianova N.F., Gilvanova E.A., Kuzmina L.Y., Melentiev A.I., Baymiev A.H, & Lopatin S.A. (2022). Constitutive chitosanase from Bacillus thuringiensis B-387 and its potential for preparation of antimicrobial chitooligomers. World journal of microbiology & biotechnology, 38(10).

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Chitosan and Chitin Preparation Protocol

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Актуганов Г.Э., Safina V., Galimzianova N., Gilvanova E., Kuzmina L.Y., Melentiev A., Baymiev A., & Лопатин С.А. (2022). Constitutive Chitosanase from Bacillus Thuringiensis B-387 and its Potential for Preparation of Antimicrobial Chitooligomers.

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