Search results for: Novozym 435
Commenced in January 2007
Frequency: Monthly
Edition: International
Paper Count: 4

Search results for: Novozym 435

4 Bioconversion of Capsaicin Using the Optimized Culture Broth of Lipase Producing Bacterium of Stenotrophomonas maltophilia

Authors: Doostishoar Farzad, Forootanfar Hamid, Hasan-Bikdashti Morvarid, Faramarzi Mohammad Ali, Ameri Atefe

Abstract:

Introduction: Chili peppers and related plants in the family of capsaicum produce a mixture of capsaicins represent anticarcinogenic, antimutagenic, and chemopreventive properties. Vanillylamine, the main product of capsaicin hydrolysis is applied as a precursor for manufacturing of natural vanillin (a famous flavor). It is also used in the production of synthetic capsaicins harboring a wide variety of physiological and biological activities such as antibacterial and anti-inflammatory effects as well as enhancing of adrenal catecholamine secretion, analgesic, and antioxidative activities. The ability of some lipases, such as Novozym 677 BG and Novozym 435 and also some proteases e.g. trypsine and penicillin acylase, in capsaicin hydrolysis and green synthesis of vanillylamine has been investigated. In the present study the optimized culture broth of a newly isolated lipase-producing bacterial strain (Stenotrophomonas maltophilia) applied for the hydrolysis of capsaicin. Materials and methods: In order to compare hydrolytic activity of optimized and basal culture broth through capsaicin 2 mL of each culture broth (as sources of lipase) was introduced to capsaicin solution (500 mg/L) and then the reaction mixture (total volume of 3 mL) was incubated at 40 °C and 120 rpm. Samples were taken every 2 h and analyzed for vanillylamine formation using HPLC. Same reaction mixture containing boiled supernatant (to inactivate lipase) designed as blank and each experiment was done in triplicate. Results: 215 mg/L of vanillylamine was produced after the treatment of capsaicin using the optimized medium for 18 h, while only 61 mg/L of vanillylamine was detected in presence of the basal medium under the same conditions. No capsaicin conversion was observed in the blank sample, in which lipase activity was suppressed by boiling of the sample for 10 min. Conclusion: The application of optimized broth culture for the hydrolysis of capsaicin led to a 43% conversion of that pungent compound to vanillylamine.

Keywords: Capsaicin, green synthesis, lipase, stenotrophomonas maltophilia

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3 Study of Individual Parameters on the Enzymatic Glycosidation of Betulinic Acid by Novozyme-435

Authors: A. U. Adamu, Hamisu Abdu, A. A. Saidu

Abstract:

The enzymatic synthesis of 3-O-β-D-glucopyranoside-betulinic acid using Novozyme-435 as a catalyst was studied. The effect of various parameters such as substrate molar ratio, reaction temperature, reaction time, re-used enzymes and amount of enzymes were investigated. The optimum rection conditions for the enzymatic glycosidation of betulinic acid in an organic solvent using Novozym-435 was found to be at 1:1.2 substrate molar ratio, 55oC, 24 h and 180 mg of enzymes with percentage conversion of 88.69 %.

Keywords: betulinic acid, glycosidation, novozyme-435, optimization

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2 Enzymatic Synthesis of Olive-Based Ferulate Esters: Optimization by Response Surface Methodology

Authors: S. Mat Radzi, N. J. Abd Rahman, H. Mohd Noor, N. Ariffin

Abstract:

Ferulic acid has widespread industrial potential by virtue of its antioxidant properties. However, it is partially soluble in aqueous media, limiting their usefulness in oil-based processes in food, cosmetic, pharmaceutical, and material industry. Therefore, modification of ferulic acid should be made by producing of more lipophilic derivatives. In this study, a preliminary investigation of lipase-catalyzed trans-esterification reaction of ethyl ferulate and olive oil was investigated. The reaction was catalyzed by immobilized lipase from Candida antarctica (Novozym 435), to produce ferulate ester, a sunscreen agent. A statistical approach of Response surface methodology (RSM) was used to evaluate the interactive effects of reaction temperature (40-80°C), reaction time (4-12 hours), and amount of enzyme (0.1-0.5 g). The optimum conditions derived via RSM were reaction temperature 60°C, reaction time 2.34 hours, and amount of enzyme 0.3 g. The actual experimental yield was 59.6% ferulate ester under optimum condition, which compared well to the maximum predicted value of 58.0%.

Keywords: ferulic acid, enzymatic synthesis, esters, RSM

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1 A Two-Stage Process for the Sustainable Production of Aliphatic Polyesters

Authors: A. Douka, S. Vouyiouka, L. M. Papaspyridi, D. Korres, C. Papaspyrides

Abstract:

A "green" process was studied for the preparation of partially renewable aliphatic polyesters based on 1,4-butanediol and 1,8-octanediol with various diacids and derivatives, namely diethyl succinate, adipic acid, sebacic acid, 1,12-dodecanedioic acid and 1,14-tetradecanedioic acid. A first step of enzymatic prepolymerization was carried out in the presence of two different solvents, toluene and diphenylether, applying molecular sieves and vacuum, respectively, to remove polycondensation by-products. Poly(octylene adipate) (PE 8.6), poly(octylene dodecanate)(PE 8.12) and poly(octylene tetradecanate) (PE 8.14) were firstly enzymatically produced in toluene using molecular sieves giving however, low-molecular-weight products. Thereafter, the synthesis of PE 8.12 and PE 8.14 was examined under optimized conditions using diphenylether as solvent and a more vigorous by-product removal step, such as application of vacuum. Apart from these polyesters, the optimized process was also implemented for the production of another long-chain polyester-poly(octylene sebacate) (PE 8.10) and a short-chain polyester-poly(butylene succinate) (PE 4.4). Subsequently, bulk post-polymerization in the melt or solid state was performed. SSP runs involved absence of biocatalyst and reaction temperatures (T) in the vicinity of the prepolymer melting point (Tm-T varied between 15.5 up to 4oC). Focusing on PE 4.4 and PE 8.12, SSP took place under vacuum or flowing nitrogen leading to increase of the molecular weight and improvement of the end product physical appearance and thermal properties.

Keywords: aliphatic polyester, enzymatic polymerization, solid state polymerization, Novozym 435

Procedia PDF Downloads 290