Journal articles: 'Novozym'

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Ortiz, Claudia, María Luján Ferreira, Oveimar Barbosa, José C. S. dos Santos, Rafael C. Rodrigues, Ángel Berenguer-Murcia, Laura E. Briand, and Roberto Fernandez-Lafuente. "Novozym 435: the “perfect” lipase immobilized biocatalyst?" Catalysis Science & Technology 9, no. 10 (2019): 2380–420. http://dx.doi.org/10.1039/c9cy00415g.

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Nyari, Nádia Ligianara Dewes, Josiane B. da Silva, Tainára Orlando, Suelen P. Piazza, Rogério L. Cansian, Débora De Oliveira, Jamile Zeni, Rogério M. Dallago, and Natália Paroul. "Processo enzimático para produção de acetato de isoamila livre de solvente orgânico." Brazilian Journal of Food Research 10, no. 1 (December 31, 2019): 129. http://dx.doi.org/10.3895/rebrapa.v10n1.9037.

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Nos últimos anos, a crescente demanda por produtos naturais na indústria de alimentos incentivou esforços notáveis no desenvolvimento de processos biotecnológicos para a produção de compostos aromatizantes. O presente estudo relata a maximização da produção de acetato de isoamila por esterificação de álcool isoamílico e ácido acético em um sistema isento de solventes usando duas lipases diferentes como catalisador. A lipase Novozyme NZL-102-LYO-HQ (Candida antarctica B imobilizada em poliuretano – PU) foi comparada com a comercializada Novozym 435 e foi avaliada em termos de desempenho, rendimento e estabilidade operacional. Os efeitos nas taxas de reação mostraram valores maximizados diferentes, empregando esses dois catalisadores, no entanto as condições reacionais no que se refere a razão molar do substrato (ácido acético: álcool isoamílico), massa de catalisador e tempo de reação foram distintos. Embora Novozym 435 exibisse maior conversão inicial com relação a NZL-102-LYO-HQ, ambas formas lineares e apresentaram uma conversão superior a 90%. Para o catalisador Novozym 435 (razão molar 1:3 de ácido acético:álcool isoamílico e massa de catalisador 17% em peso) em 240 minutos e a Novozyme NZL-102-LYO-HQ (Candida antarctica B imobilizada em poliuretano – PU) (razão molar 1:5 de ácido acético:álcool isoamílico e massa de catalisador 7% em peso) em 360 minutos de reação com 10 ciclos de reutilização. Sendo assim esses resultados são de grande valia para a produção industrial, sobretudo na síntese de ésteres de cadeia média, como acetato de isoamila em diferentes preparações enzimáticas, tornando uma fonte promissora comparado com estudo apresentados na literatura aberta.

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Manurung, Renita, and Alwi Gery Siregar. "Reusability of the Deep Eutectic Solvent - Novozym 435^® Enzymes System in Transesterification from Degumming Palm Oil." Advanced Engineering Forum 35 (February 2020): 9–17. http://dx.doi.org/10.4028/www.scientific.net/aef.35.9.

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In this study, deep eutectic solvent (DES) used as co solvent for enzymatic biodiesel production from degumming palm oil (DPO). DES is formed from the salt compound choline-chloride (ChCI) with glycerol at 1:2 molar ratio. Furthermore, the effectiveness of the DES was tested by enzymatic reactions using novozym 435® for the production of palm biodiesel with raw materials DPO. The use of enzymes with the DES system can maintain the activity and stability of the novozyme enzyme measured by the yield produced until the 10th usage produces biodiesel yield > 99% with a concentration of DES 0.5% with a molar ratio of 0.5% water. Spectra of DES ChCI:glycerol and ChCI:glycerol:water characterized by FTIR, morphological structure novozym by characterized SEM and then biodiesel product analyzed by GC-MS. This shows that the ChCI:glycerol:water system in enzymatic biodiesel production has good potential to maintain enzyme activity and stability.

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Zou, Cheng, You Yan Liu, Yi Ming Qin, Ai Xing Tang, and Li Na Lan. "Chemoenzymatic Epoxidation of α-Pinene Catalyzed by Novozym 435." Advanced Materials Research 634-638 (January 2013): 896–900. http://dx.doi.org/10.4028/www.scientific.net/amr.634-638.896.

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The synthesis of α-pinene oxide mediated by Novozym 435 (lipase from Candida antarctica) in a three-phase system was studied in this work. Novozyme 435 catalysed the formation of peroxyoctanoic acid directly from octanoic acid and hydrogen peroxide, which was then applied for in situ oxidation of α-pinene. The highest conversion of a-pinene (approximately 80%) was obtained when the reaction was performed at 30°C and initial hydrogen peroxide concentration in the water phase was set to be 30%. The parameters affecting the lipase activity were also investigated，where the peracid generated in organic phase was obvserved to greatly inactivate the enzyme compared to other components in the organic phase.

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Prošková, A., Z. Kopicová, J. Kučera, and L. Škarková. "Lipase-catalyzed transesterification of rendering plant fat – Short Communication." Research in Agricultural Engineering 56, No. 3 (August 26, 2010): 122–25. http://dx.doi.org/10.17221/40/2009-rae.

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Soluble lipase (Lipozyme CALB L) was immobilized by covalent bond to chitosan pellets prepared from Aspergillus niger mycelium. This immobilized enzyme was compared with commercial immobilized lipase of the same origin (Novozym 435). Novozym 435 is also lipase CALB L commercially immobilized by sorption on poly-(methyl acrylate). Novozym 435 shows much higher conversion of rendering plant fat in methanol under optimum conditions, having, at the same time, lower optimum temperature and lower stability at higher temperature. Lipozyme CALB L immobilized on chitosan leads to a low conversion, regardless its higher thermal stability. Novozym 435 gives conversion of about 50% of theoretical value, which is in good accordance with basically catalyzed transesterification of rendering plant fat described elsewhere. Lipozyme CALB L immobilized on chitosan gives conversion of about 10% of theoretical value only. The use of Novozym 435 in two-step system (enzyme-acid) seems to be more convenient compared with traditional two-step system (base-acid)

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Dalla Rosa, Clarissa, Débora de Oliveira, and José Vladimir Oliveira. "The role of organic solvent amount in the lipase-catalyzed biodiesel production." Food Science and Technology 30, no. 1 (February 26, 2010): 76–78. http://dx.doi.org/10.1590/s0101-20612010005000008.

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This research note addresses the role of organic solvent amount in the production of fatty acid ethyl esters from soybean oil. N-hexane was chosen as solvent and two commercial immobilized lipases as catalysts, Novozym 435 and Lipozyme IM. The reactions were conducted in 6 hours, varying the solvent to oil ratio from zero to 50 (v/wt) and adopting adopting for Novozym 435: 65 ºC, enzyme concentration (E, wt%) = 5, oil to ethanol molar ratio (R) = 1:10, water addition (H, wt%) = 0, and for Lipozyme IM: 35 ºC, E = 5 wt%, R = 1:3, H = 10 wt%. For Lipozyme IM, an increase in solvent amount is shown to lead to an enhancement of reaction conversion, while a negligible effect was found for Novozym 435. When using 30 mL of solvent the reaction conversions were 88% for Lipozyme IM and 15% for Novozym 435.

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Aguieiras, Erika C. G., Cláudia O. Veloso, Juliana V. Bevilaqua, Danielle O. Rosas, Mônica A. P. da Silva, and Marta A. P. Langone. "Estolides Synthesis Catalyzed by Immobilized Lipases." Enzyme Research 2011 (June 20, 2011): 1–7. http://dx.doi.org/10.4061/2011/432746.

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Estolides are vegetable-oil-based lubricants obtained from oleic acid or any source of hydroxy fatty acids. In this work, the estolides synthesis from oleic acid and methyl ricinoleate (biodiesel from castor oil), using immobilized commercial lipases (Novozym 435, Lipozyme RM-IM, and Lipozyme TL-IM) in a solvent-free medium was investigated. Acid value was used to monitor the reaction progress by determining the consumption of acid present in the medium. Novozym 435 showed the best performance. Water removal improved the conversion. Novozym 435 was more active at atmospheric pressure. Novozym 435 was reused four times with conversion reaching 15% after the fourth reaction at 80°C. Estolides produced under the reaction conditions used in this work presented good properties, such as, low temperature properties as pour point (−24°C), viscosity (23.9 cSt at 40°C and 5.2 cSt at 100°C), and viscosity index (153).

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Moreira, Katerine S., Lourembergue S. Moura Júnior, Rodolpho R. C. Monteiro, André L. B. de Oliveira, Camila P. Valle, Tiago M. Freire, Pierre B. A. Fechine, et al. "Optimization of the Production of Enzymatic Biodiesel from Residual Babassu Oil (Orbignya sp.) via RSM." Catalysts 10, no. 4 (April 9, 2020): 414. http://dx.doi.org/10.3390/catal10040414.

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Residual oil from babassu (Orbignya sp.), a low-cost raw material, was used in the enzymatic esterification for biodiesel production, using lipase B from Candida antarctica (Novozym® 435) and ethanol. For the first time in the literature, residual babassu oil and Novozym® 435 are being investigated to obtain biodiesel. In this communication, response surface methodology (RSM) and a central composite design (CCD) were used to optimize the esterification and study the effects of four factors (molar ratio (1:1–1:16, free fatty acids (FFAs) /alcohol), temperature (30–50 °C), biocatalyst content (0.05–0.15 g) and reaction time (2–6 h)) in the conversion into fatty acid ethyl esters. Under optimized conditions (1:18 molar ratio (FFAs/alcohol), 0.14 g of Novozym® 435, 48 °C and 4 h), the conversion into ethyl esters was 96.8%. It was found that after 10 consecutive cycles of esterification under optimal conditions, Novozym® 435 showed a maximum loss of activity of 5.8%, suggesting a very small change in the support/enzyme ratio proved by Fourier Transform Infrared (FTIR) spectroscopy and insignificant changes in the surface of Novozym® 435 proved by scanning electron microscopy (SEM) after the 10 consecutive cycles of esterification.

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Sørensen, Annette, Peter Stephensen Lübeck, Mette Lübeck, Philip Johan Teller, and Birgitte Kiær Ahring. "β-Glucosidases from a new Aspergillus species can substitute commercial β-glucosidases for saccharification of lignocellulosic biomass." Canadian Journal of Microbiology 57, no. 8 (August 2011): 638–50. http://dx.doi.org/10.1139/w11-052.

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β-Glucosidase activity plays an essential role for efficient and complete hydrolysis of lignocellulosic biomass. Direct use of fungal fermentation broths can be cost saving relative to using commercial enzymes for production of biofuels and bioproducts. Through a fungal screening program for β-glucosidase activity, strain AP (CBS 127449, Aspergillus saccharolyticus ) showed 10 times greater β-glucosidase activity than the average of all other fungi screened, with Aspergillus niger showing second greatest activity. The potential of a fermentation broth of strain AP was compared with the commercial β-glucosidase-containing enzyme preparations Novozym 188 and Cellic CTec. The fermentation broth was found to be a valid substitute for Novozym 188 in cellobiose hydrolysis. The Michaelis–Menten kinetics affinity constant as well as performance in cellobiose hydrolysis with regard to product inhibition were found to be the same for Novozym 188 and the broth of strain AP. Compared with Novozym 188, the fermentation broth had higher specific activity (11.3 U/mg total protein compared with 7.5 U/mg total protein) and also increased thermostability, identified by the thermal activity number of 66.8 vs. 63.4 °C for Novozym 188. The significant thermostability of strain AP β-glucosidases was further confirmed when compared with Cellic CTec. The β-glucosidases of strain AP were able to degrade cellodextrins with an exo-acting approach and could hydrolyse pretreated bagasse to monomeric sugars when combined with Celluclast 1.5L. The fungus therefore showed great potential as an onsite producer for β-glucosidase activity.

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Aguilera-Oviedo, Johanna, Edinson Yara-Varón, Mercè Torres, Ramon Canela-Garayoa, and Mercè Balcells. "Sustainable Synthesis of Omega-3 Fatty Acid Ethyl Esters from Monkfish Liver Oil." Catalysts 11, no. 1 (January 13, 2021): 100. http://dx.doi.org/10.3390/catal11010100.

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The search for economic and sustainable sources of polyunsaturated fatty acids (PUFAs) within the framework of the circular economy is encouraged by their proven beneficial effects on health. The extraction of monkfish liver oil (MLO) for the synthesis of omega-3 ethyl esters was performed to evaluate two blending systems and four green solvents in this work. Moreover, the potential solubility of the MLO in green solvents was studied using the predictive simulation software COnductor-like Screening MOdel for Realistic Solvents (COSMO-RS). The production of ethyl esters was performed by one or two-step reactions. Novozym 435, two resting cells (Aspergillus flavus and Rhizopus oryzae) obtained in our laboratory and a mix of them were used as biocatalysts in a solvent-free system. The yields for Novozym 435, R. oryzae and A. flavus in the one-step esterification were 63, 61 and 46%, respectively. The hydrolysis step in the two-step reaction led to 83, 88 and 93% of free fatty acids (FFA) for Novozym 435, R. oryzae and A. flavus, respectively. However, Novozym 435 showed the highest yield in the esterification step (85%), followed by R. oryzae (65%) and A. flavus (41%). Moreover, selectivity of polyunsaturated fatty acids of R. oryzae lipase was evidenced as it slightly esterified docosahexaenoic acid (DHA) in all the esterification reactions tested.

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Sun, Shangde, and Liya Tian. "Novozym 40086 as a novel biocatalyst to improve benzyl cinnamate synthesis." RSC Advances 8, no. 65 (2018): 37184–92. http://dx.doi.org/10.1039/c8ra08433e.

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Mulalee, Sawittree, Karnjana Sena, and Muenduen Phisalaphong. "Enzymatic Esterification of Oleic Acid and Propanol by Novozym 435." Applied Mechanics and Materials 705 (December 2014): 29–33. http://dx.doi.org/10.4028/www.scientific.net/amm.705.29.

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Recently, demand of biolubricants has been continuously increased since it is environmentally friendly and renewable. Therefore, this research focused on the biolubricants production from enzymatic esterification of oleic acid and propanol using Novozym 435 as a biocatalyst. The esterification experiments were conducted under the optimal conditions, as follows: 45°C, oleic acid to propanol molar ratio of 1:2, Novozym 435 loading of 5% based on the weight of oleic acid. It was shown that the optimal rotation speed at 250 rpm could minimize the effect of external mass transfer limitations and maintained the enzyme activity. The conversion of oleic acid from the esterification for 6 h with isopropanol was 76.4%, which was lower than that with n-propanol (88.9%). Novozym 435 could be reused in the production of propyloleate for at least 5 cycles with maintaining FFA conversion of 94% of its initial value. Moreover, the use of molecular sieve to remove water during the reaction could significantly enhance the final FFA conversion from 88.9% to 94.7%.

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Wang, Hongjiang, Zebiao Li, Xiaoxia Yu, Ruidong Chen, Xiulai Chen, and Liming Liu. "Green synthesis of (R)-3-TBDMSO glutaric acid methyl monoester using Novozym 435 in non-aqueous media." RSC Advances 5, no. 92 (2015): 75160–66. http://dx.doi.org/10.1039/c5ra14348a.

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Zhang, Jia Chan, Chan Zhang, Lei Zhao, and Cheng Tao Wang. "Lipase-Catalyzed Synthesis of Sucrose Fatty Acid Ester and the Mechanism of Ultrasonic Promoting Esterification Reaction in Non-Aqueous Media." Advanced Materials Research 881-883 (January 2014): 35–41. http://dx.doi.org/10.4028/www.scientific.net/amr.881-883.35.

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The preparation of sucrose fatty acid ester (SFAE) by lipase-catalyzing reaction usingCandida antarcticalipase B (CalB) and its immobilized form Novozym 435 was reported in this work. The preparation was characterized in non-aqueous media with and without ultrasound irradiation treatment. A conversion rate of SFAE up to 49.60% was achieved using Novozym 435 under the optimal conditions (45.4°C; mole ratio of methyl oleate to sucrose = 6.0:1; 4.0 mL acetone; 4.0 mg/mL Novozym 435; and 24.6 h of reaction). Under optimal ultrasound conditions (50 kHz, 0.15 W/cm2, 166.55 min), reaction time decreased by 75% approximately, compared with the control without ultrasonic irradiation, but the ultrasound irradiation treatment did not affect the SFAE yield catalyzed by Novozym 435. In the CalB-catalyzed preparation of SFAE under the same optimal reaction conditions, ultrasonic irradiation enhanced the activity of CalB during early time points and inhibited its activity after a long period of treatment. Moreover, CalB was further examined using Far-UV circular dichroism (CD) spectroscopy and scanning electron microscopy (SEM) to study the conformation and micro-morphology of CalB structural variations in various ultrasound irradiation treatments. CD results indicated that α-helical regions were increased and random coil regions remained at a similar level of proportion. SEM images showed small holes appeared on the surface of irradiated CalB. Therefore, we conclude that proper ultrasound irradiation could change the secondary structure and the surface morphology of the CalB in molecular level, and could accelerate the esterification reaction process.

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Mat Radzi, Salina, Nurul Jannah Abd Rahman, Hanina Mohd Noor, and Norlelawati Ariffin. "Improvement on the Catalytic Performance Using Dual Lipases System in the Synthesis of Ferulate Esters." Applied Mechanics and Materials 754-755 (April 2015): 902–6. http://dx.doi.org/10.4028/www.scientific.net/amm.754-755.902.

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A novel approach of dual lipases system was successfully carried out in improving the synthesis of ferulate esters between ethyl ferulate and olive oil. Combination of Novozym 435 and Lipozyme RMIM were used as biocatalyst to improve the reaction performance. Different reaction parameters (ratio of lipases, reaction time, lipase dosage, substrate molar ratio and reaction temperature) were analyzed systematically. A high conversion of ferulate esters (85%) was obtained after 12 hrs of reaction time at optimal conditions of 1:9 w/w (Novozym 435/Lipozyme RMIM), 80 mg of lipase and 1:4 ethyl ferulate:olive oil at 60 oC.

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Mulalee, Sawittree, Jiranan Chanprasert, Piboon Kerdpoksup, Netnapa Sawangpanya Sawangpanya, and Muenduen K. M. Phisalaphong. "Esterification of Oleic Acid and Bioalcohols Using Immobilized Lipase." Advanced Materials Research 724-725 (August 2013): 1154–57. http://dx.doi.org/10.4028/www.scientific.net/amr.724-725.1154.

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Biodiesel has been receiving significant attention as a renewable and nonpolluting fuel. In this study, oleic acid and bioalcohols (ethanol and butanol) were used as substrates for biodiesel production. The reactions were performed in a solvent-free system using immobilized lipase (Novozym 435) as biocatalyst in a batch esterification process. The optimal conditions were 45°C, oleic acid to alcohol molar ratio of 1:2, Novozym 435 loading at 5% based on oleic acid weight and 250 rpm, in which the free fatty acid (FFA) conversion at 91.0% was obtained after 12 hours of the reaction.

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Beran, M., J. Pinkrová, M. Urban, and J. Drahorád. "Immobilisation of endoinulinase on polyhydroxybutyrate microfibers." Czech Journal of Food Sciences 34, No. 6 (December 21, 2016): 541–46. http://dx.doi.org/10.17221/72/2016-cjfs.

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Due to the health benefits associated with the consumption of prebiotic short-chain fructooligosaccharides (sc-FOS) and inulooligosaccharides (IOS), there is increased interest in the use of these compounds in food products. We have developed a new biocatalyst for the production of FOS and IOS by inulin hydrolysis. Endoinulinase from Aspergillus niger Inulinase® Novozym 960 (Novozymes) was immobilised on polyhydroxybutyrate (PHB) nanofibres and microfibres by hydrophobic interactions. The PHB fibres were prepared by centrifugal spinning. FOS and IOS profiles were determined by ion-exchange chromatography with the Rezex RSO-Oligosaccharide column. The biocatalyst had very good activity and stability after repeated applications. It can be used in biocatalytic membrane reactors for the production of prebiotic oligosaccharides.

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Fredes, Yerko, Lesly Chamorro, and Zaida Cabrera. "Increased Selectivity of Novozym 435 in the Asymmetric Hydrolysis of a Substrate with High Hydrophobicity Through the Use of Deep Eutectic Solvents and High Substrate Concentrations." Molecules 24, no. 4 (February 22, 2019): 792. http://dx.doi.org/10.3390/molecules24040792.

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The effects of the reaction medium and substrate concentration were studied on the selectivity of Novozym 435 using the asymmetric hydrolysis of dimethyl-3-phenylglutarate as a model reaction. Results show that the use of choline chloride ChCl:urea/phosphate buffer 50% (v/v) as a reaction medium increased the selectivity of Novozym 435 by 16% (e.e = 88%) with respect to the one in 100% phosphate buffer (e.e = 76%). Best results were obtained when high substrate concentrations (well above the solubility limit, 27-fold) and ChCl:urea/phosphate buffer 50% (v/v) as reaction medium at pH 7 and 30 °C were used. Under such conditions, the R-monoester was produced with an enantiomeric purity of 99%. Novozym 435 was more stable in ChCl:urea/phosphate buffer 50% (v/v) than in phosphate buffer, retaining a 50% of its initial activity after 27 h of incubation at pH 7 and 40 °C. Results suggest that the use of deep eutectic solvents (ChCl:urea/phosphate buffer) in an heterogeneous reaction system (high substrate concentration) is a viable and promising strategy for the synthesis of chiral drugs from highly hydrophobic substrates.

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Liu, W., and F. Duan. "Lipase-catalyzed transesterification of epoxidized soybean oil to prepare epoxy methyl esters." Grasas y Aceites 69, no. 2 (June 4, 2018): 247. http://dx.doi.org/10.3989/gya.1103172.

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Epoxidized soybean oil methyl esters could be efficiently prepared with the transesterification of epoxidized soybean oil (ESBO) with a lower dosage of methanol using lipase Novozym 435 as catalyst. The optimum parameters were as follows: the molar ratio of 5:1 (methanol to ESBO), 5% Novozym 435 as catalyst, at 45 °C for 14 h, with a stirring speed of 600rpm, under which the epoxidized soybean oil methyl esters (ESBOME) could be obtained at a 95.7% yield. During the enzymatic transesterification process, the oxirane oxygen values were kept unchangeable, which indicated that excellent functional group tolerance could be achieved under such mild reaction conditions. In addition, the recyclability of the immobilized enzyme Novozym 435 in this transesterification process was examined and the results showed that the biocatalyst could be reused ten times without losing any reaction activity or selectivity. And the final products of ESBOME were also identified by IR and NMR analysis. The kinetic data obtained followed the Ping-Pong Bi mechanism model (Vmax = 6.132 mol·L-1min-1, Km,S = 0,0001 mol·L-1, Km, A = 796.148 mol·L-1, Ki, A = 0,0004 mol·L-1) with competitive inhibition by methanol.

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Gruczynska-Sekowska, E., F. Aladedunye, F. Anwar, P. Koczon, D. Kowalska, M. Kozlowska, E. Majewska, and K. Tarnowska. "Development of zero-trans shortenings with high thermo-oxidative stability by enzymatic transesterification." Grasas y Aceites 71, no. 4 (December 30, 2020): 375. http://dx.doi.org/10.3989/gya.0564191.

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Novel zero-trans frying shortenings were formed by enzymatic transesterification by exploring a palm stearin and canola oil mixture and stearic acid as substrates. Both immobilized (Novozym 435, Lipase PS “Amano” IM) and non-immobilized (Lipomod TM 34P) enzymes were applied as biocatalysts. Palmitic acid, the fatty acid which defines the proper type of crystal formation, was present at the 15% level in the reaction mixtures. The novel structured lipids had comparable physical properties and offered similar frying performance to those of commercial shortening. Needle-shaped crystals were predominant both in the transesterification products and the commercial frying shortening. Furthermore, solid fat content profiles of the zero-trans structured lipids produced by Novozym 435 and Lipase PS “Amano” IM were close to those of the commercial shortening.

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Yamamoto, Yuuko, Yoshihiko Akakabe, Kenji Matsui, Hiroshi Shimidzu, and Tadahiko Kajiwara. "Chemo-Enzymatic Syntheses of Both Enantiomers of Neodictyoprolenol and Neodictyoprolene; Possible Biosynthetic Intermediates of Sex Pheromones in Brown Algae." Zeitschrift für Naturforschung C 54, no. 12 (December 1, 1999): 1027–32. http://dx.doi.org/10.1515/znc-1999-1206.

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Neodictyoprolenol [(-)-(S)-(1,5Z,8Z)-undecatrien-3-ol], dictyoprolenol [(-)-(S )-(1,5Z)- undecadien-3-ol] and their acetates neodictyoprolene [(+)-(5)-3-acetoxy-(1,5Z,8Z)-undecatriene] and dictyoprolene [(+)-(S)-3-acetoxy-(1,5Z)-undecadiene], which are interesting as possible biosynthetic intermediates of the sex pheromones (dictyopterene B, C′ and D′) of brown algae, were synthesized by chemo-enzymatic methods through optical resolution of racemic neodictyoprolenol and dictyoprolenol using two lipases; Amano PS (Pseudom onas sp.) and Novozym 435® (Candida sp.). A combination of acylation of the alcohols and hydrolysis of the acetates by Novozym 435® produced neodictyoprolenol, neodictyoprolene, dictyoprolenol and dictyoprolene with high optical purities over 99% enantiomeric excess (e.e.). This snythetic methods will make it easier to search these compounds in marine algae and to study their biosynthesis.

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Pascalis Novalina, Arya Josua S, Taslim, and Tjahjono Herawan. "PENGARUH VARIASI VARIABEL REAKSI PADA PROSES EKSTRAKSI REAKTIF MESOKARP SAWIT UNTUK MENGHASILKAN BIODIESEL." Jurnal Teknik Kimia USU 4, no. 4 (December 24, 2015): 18–24. http://dx.doi.org/10.32734/jtk.v4i4.1509.

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The conventional method for the production of biodiesel needed the oil that is extracted from the biomass before it can be transesterified into fatty acid methyl esters (FAME). Reactive extraction can be used to produce biodiesel with high-yield, low production costs, reduce the reaction time and the use of reagents and co-solvents, making it easier to produce biodiesel. In this study, reactive extraction applied to produce biodiesel from palm fruit mesocarp extracted using dimethyl carbonate as a solvent and reagents, and novozym®435 as a catalyst. Methanol was replaced by dialkyl carbonates, particularly dimethyl carbonate. Dimethyl carbonate can be used as a solvent and as a reagent, so reactive extraction is very easy to apply. The parameters will be study are reaction temperature (50, 60, and 70 °C), reaction time (8, 16, 24 hours), the molar ratio of reactants (50: 1, 60: 1, 70: 1 n/n ), the concentration of novozym® 435 (5%, 10%, 15% wt).The results showed that the highest biodiesel yield can be achivied at conditions temperature of 60 °C, reaction time 24 hours, molar ratio of reactants palm mesocarp to DMC 1:60, and novozym®435 concentration of 10wt%. The results showed that the synthesis of biodiesel via reactive extraction using palm mesocarp as raw material requires a low production cost.

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Khatri, Vinod, Sumati Bhatia, Satyanarayan Deep, Ekta Kohli, Rainer Haag, Nihar Nalini Senapati, and Ashok K. Prasad. "Exploring hydrophobic diastereomeric 2,6-anhydro-glycoheptitols for their enzymatic polymerization with PEG: towards delivery applications." New Journal of Chemistry 44, no. 36 (2020): 15369–75. http://dx.doi.org/10.1039/d0nj02642e.

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Two sugar PEG-based amphiphilic copolymers have been synthesized by Novozym®-435-catalyzed greener solvent free transesterification reaction of diastereomeric 2,6-anhydro-glucoheptitol and 2,6-anhydro-mannoheptitol with PEG-1000 diethyl ester.

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Corrêa, Igor Nascentes dos Santos, Susana Lorena de Souza, Marly Catran, Otávio Luiz Bernardes, Márcio Figueiredo Portilho, and Marta Antunes Pereira Langone. "Enzymatic Biodiesel Synthesis Using a Byproduct Obtained from Palm Oil Refining." Enzyme Research 2011 (May 26, 2011): 1–8. http://dx.doi.org/10.4061/2011/814507.

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An alternative route to produce biodiesel is based on esterification of free fatty acids present in byproducts obtained from vegetable oil refining, such as palm oil fatty acid distillate (PFAD). PFAD is a byproduct of the production of edible palm oil, which contains 96 wt.% of free fatty acids. The purpose of this work was to study biodiesel synthesis via esterification of PFAD with methanol and ethanol, catalyzed by commercial immobilized lipases (Novozym 435, Lipozyme RM-IM, and Lipozyme TL-IM), in a solvent-free system. The effects of reaction parameters such as type of lipase, enzyme amount, type of alcohol, alcohol amount, and enzyme reuse were studied. Fatty acid conversion of 93% was obtained after 2.5 h of esterification reaction between PFAD and ethanol using 1.0 wt.% of Novozym 435 at 60°C.

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Ribeiro, Bernardo Dias, Lucas de Carvalho Iff, Maria Alice Zarur Coelho, and Isabel M. Marrucho. "Influence of Betaine- and Choline-based Eutectic Solvents on Lipase Activity." Current Biochemical Engineering 5, no. 1 (September 27, 2019): 57–68. http://dx.doi.org/10.2174/2212711906666190710181629.

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Background: Eutectic solvents are a mixture of two compounds which possess a lower melting temperature than the parent compounds, using quaternary ammonium salts, such as choline chloride and betaine hydrochloride and organic acids, polyols and amides as hydrogen bond donors. These solvents can be an alternative as non-aqueous media for enzymatic reactions, mainly using lipases. Objective: The objective of this work is to evaluate enzymatic activity and stability of commercial lipases, immobilized or at free form (Thermomyces lanuginosus: Lipozyme TL IM, iTL and Lipolase 100 L, fTL; Candida antarctica: Novozym 435, iCALB; Novozym 735, iCALA and Novozym CALB L, fCALB); and a phospholipase (Lecitase Ultra), in the presence of eutectic solvents (choline chloride ChCl:urea, ChCl:glycerol, betaine hydrochloride (BeHCl):urea and BeHCl: glycerol. Methods: Initially, lipases were maintained for 2 hours in solutions of choline and betaine-based eutectic solvents (1 to 20% m/m) at 25ºC compared with water for relative enzymatic activity. Using the solvent that best promoted lipase activity, some parameters were evaluated such as the molar ratio between quaternary ammonium salts and urea, stocking temperature and kinetics. Results and Conclusion: These eutectic solvents enable, mainly with immobilized lipases, 25 to 125 times more activity than water at 25ºC and 2h, and even after 24h, lipase iTLL was still 40 times more active in the presence of ChCl:Urea 1:3. Lipase iCALB showed great thermostability 47 times higher at 55ºC, almost double relative activity at 25ºC in the presence of BetHCl:Urea 1:4.

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Yadav, Ganapati D., and K. Manjula Devi. "Enzymatic synthesis of perlauric acid using Novozym 435." Biochemical Engineering Journal 10, no. 2 (March 2002): 93–101. http://dx.doi.org/10.1016/s1369-703x(01)00164-4.

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Shaw, J. F., S. W. Chang, S. C. Lin, T. T. Wu, H. Y. Ju, C. C. Akoh, R. H. Chang, and C. J. Shieh. "Continuous Enzymatic Synthesis of Biodiesel with Novozym 435." Energy & Fuels 22, no. 2 (March 2008): 840–44. http://dx.doi.org/10.1021/ef7005047.

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O'BRIEN, GERALDINE A., and PETER A. WHITTAKER. "Regeneration of yeast protoplasts prepared using Novozym 234." Biochemical Society Transactions 18, no. 2 (April 1, 1990): 328–29. http://dx.doi.org/10.1042/bst0180328.

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Veld, Martijn A. J., Anja R. A. Palmans, and E. W. Meijer. "Selective polymerization of functional monomers with Novozym 435." Journal of Polymer Science Part A: Polymer Chemistry 45, no. 24 (December 15, 2007): 5968–78. http://dx.doi.org/10.1002/pola.22350.

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Bhattacharya, S., A. Drews, M. Kraume, and M. B. Ansorge-Schumacher. "Kinetik einer Epoxidierung mittels silikonbeschichtetem Novozym®435." Chemie Ingenieur Technik 82, no. 9 (August 27, 2010): 1523–24. http://dx.doi.org/10.1002/cite.201050540.

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Baheti, Payal, Olinda Gimello, Cécile Bouilhac, Patrick Lacroix-Desmazes, and Steven M. Howdle. "Sustainable synthesis and precise characterisation of bio-based star polycaprolactone synthesised with a metal catalyst and with lipase." Polymer Chemistry 9, no. 47 (2018): 5594–607. http://dx.doi.org/10.1039/c8py01266k.

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Development of a sustainable route for the synthesis of star-shaped poly(ε-caprolactone) using renewable feedstocks in clean solvents (scCO₂ and bulk) with the catalysts Sn(Oct)₂ or the enzyme Novozym 435.

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Bebić, Jelena, Katarina Banjanac, Jelena Rusmirović, Marija Ćorović, Ana Milivojević, Milica Simović, Aleksandar Marinković, and Dejan Bezbradica. "Amino-modified kraft lignin microspheres as a support for enzyme immobilization." RSC Advances 10, no. 36 (2020): 21495–508. http://dx.doi.org/10.1039/d0ra03439h.

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The active biocatalyst systems were developed by immobilizing β-galactosidase from A. oryzae and laccase from M. thermophila expressed in A. oryzae (Novozym®51003) onto amino-modified microspheres based on bio-waste derived material, such as kraft lignin.

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CAMPOS, PLÍNIO R. F., APARECIDO N. MÓDENES, FERNANDO R. ESPINOZA-QUIÑONES, DANIELA E. G. TRIGUEROS, SUELI T. D. BARROS, and NEHEMIAS C. PEREIRA. "Improvement on the concentrated grape juice physico-chemical characteristics by an enzymatic treatment and Membrane Separation Processes." Anais da Academia Brasileira de Ciências 88, no. 1 (March 4, 2016): 423–36. http://dx.doi.org/10.1590/0001-3765201620140136.

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ABSTRACT In this work, the improvement on the concentrated grape juice physico-chemical characteristics by using an enzymatic treatment followed by Membrane Separation Process (MSP) has been investigated. By using Novozym 33095(r) and Ultrazym AFP L(r) enzymes varying three operating parameters, the best result on the grape pulp characteristics was attained for the Novozym 33095(r) performed at 35oC, 15 min. and 50 mgL-1. In micro/ultra filtration processes after enzymatic pretreatment, the best performance of the MSP with high permeate flux value and suitable grape juice characteristics was attained using 0.05 mm membrane pore size, 1 bar pressure and 40 oC treatment temperature. When reverse osmosis process is operated at 40 bar and 40oC, high soluble solid and low turbidity values are attained. An enzymatic treatment along with MSP has shown an alternative and efficient grape juice processing system, being possible to extend to other foods.

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Baek, Yesol, Jonghwa Lee, Jemin Son, Taek Lee, Abdus Sobhan, Jinyoung Lee, Sang-Mo Koo, Weon Ho Shin, Jong-Min Oh, and Chulhwan Park. "Enzymatic Synthesis of Formate Ester through Immobilized Lipase and Its Reuse." Polymers 12, no. 8 (August 11, 2020): 1802. http://dx.doi.org/10.3390/polym12081802.

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Octyl formate is an important substance used in the perfume industry in products such as cosmetics, perfumes, and flavoring. Octyl formate is mostly produced by chemical catalysts. However, using enzymes as catalysts has gathered increasing interest due to their environment-friendly proprieties. In the present study, we aimed to identify the optimal conditions for the synthesis of octyl formate through immobilized enzyme-mediated esterification. We investigated the effects of enzymatic reaction parameters including the type of immobilized enzyme, enzyme concentration, molar ratio of reactants, reaction temperature, and type of solvent using the optimization method of one factor at a time (OFAT). The maximum conversion achieved was 96.51% with Novozym 435 (15 g/L), a 1:7 formic acid to octanol ratio, a reaction temperature of 40 °C, and with 1,2-dichloroethane as solvent. Moreover, we demonstrated that the Novozym 435 can be reused under the optimal conditions without affecting the octyl formate yield, which could help reduce the economic burden associated with enzymatic synthesis.

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Miao, Changlin, Zhongming Wang, Lingmei Yang, Huiwen Li, Pengmei Lv, Xinshu Zhuang, Zhenhong Yuan, and Wen Luo. "Lipase-Catalyzed Synthesis of Glycerol-Free Biodiesel from Rapeseed Oil and Dimethyl Carbonate." Journal of Biobased Materials and Bioenergy 14, no. 4 (August 1, 2020): 537–43. http://dx.doi.org/10.1166/jbmb.2020.1973.

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The enzymatic production of glycerol-free biodiesel by the transesterification of rapeseed oil was studied using lipase as catalyst. A series of co-solvents were employed in an attempt to improve reaction kinetics. The effects of the reaction conditions (molar ratio of dimethyl carbonate (DMC) and rapeseed oil, type of lipases, amount of lipases, solvent effects, reaction temperature and time) on the conversion and yield of biodiesel and glycerol carbonate (GC) were investigated. The optimal conditions for biodiesel and GC were 20% Novozym 435, 3:1 molar ratio of DMC to rapeseed oil, and with 20% [Omim][BF6] as solvent. Under these conditions, the conversions of 88.51% biodiesel and 73.87% GC have been achieved after 48 h. The biodiesel and GC conversions were eight times higher compared to the conventional solvent-free system, respectively. There was no obvious loss in the biodiesel and GC yield after Novozym 435 having been used for five recycling.

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Debets, Alfons J. M., Klaas Swart, and Cees J. Bos. "Mitotic mapping in linkage group V of Aspergillus niger based on selection of auxotrophic recombinants by Novozym enrichment." Canadian Journal of Microbiology 35, no. 11 (November 1, 1989): 982–88. http://dx.doi.org/10.1139/m89-164.

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This paper describes a procedure which allows the quantitative selection of auxotrophs of the fungus Aspergillus niger by enzymatic killing of immobilized germinating prototrophic conidiospores. We have applied this procedure to linkage analysis on the basis of mitotic crossing-over in this fungus. Starting with a heterozygous diploid strain, we could select auxotrophic homozygous diploid recombinants quantitatively. We estimated the frequency of crossing-over after correction for clonal distribution of recombinants, and localized four auxotrophic markers as well as the centromere on chromosome V of this fungus. The Novozym enrichment procedure proved to be useful in genetic analysis and for the construction of recombinant genotypes in the case of closely linked auxotrophic markers. The detemination of gene order and the estimation of distances on the basis of benomyl-induced recombinant haploid segregants may lead to incorrect conclusions. Genetic analysis on the basis of homozygous recombinants, however, can provide reliable estimates of map distances.Key words: Aspergillus niger, chromosome mapping, mitotic crossing-over, Novozym enrichment, auxotrophic recombinants.

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Mukherjee, Chandrani, Prabhu P. Mohapatra, Dani Youssef, and Amitabh Jha. "Optical enrichment in enzyme-catalyzed resolution of 1-aryl-2,2-dimethyl-1,3-propanediols." Canadian Journal of Chemistry 95, no. 1 (January 2017): 1–6. http://dx.doi.org/10.1139/cjc-2016-0341.

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Novozym® 435 efficiently catalyzed the chemo-, regio-, and enantioselective transesterification of 1-aryl-2,2-dimethyl-1,3-propanediols in different organic solvents with vinyl acetate as the acetyl donor at room temperature. This enzyme-catalyzed chemical transformation method provides an efficient route for optically enriched propanediol derivatives.

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Xin, Jia-Ying, Yan Wang, Tie Liu, Kai Lin, Le Chang, and Chun-Gu Xia. "Biosysthesis of Corn Starch Palmitate by Lipase Novozym 435." International Journal of Molecular Sciences 13, no. 6 (June 12, 2012): 7226–36. http://dx.doi.org/10.3390/ijms13067226.

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Virto, Carmen, and Patrick Adlercreutz. "Lysophosphatidylcholine synthesis with Candida antarctica lipase B (Novozym 435)." Enzyme and Microbial Technology 26, no. 8 (May 2000): 630–35. http://dx.doi.org/10.1016/s0141-0229(00)00147-2.

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Chang, Hung-Min, Hui-Fen Liao, Chin-Chia Lee, and Chwen-Jen Shieh. "Optimized synthesis of lipase-catalyzed biodiesel by Novozym 435." Journal of Chemical Technology & Biotechnology 80, no. 3 (2005): 307–12. http://dx.doi.org/10.1002/jctb.1166.

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Costa Assuncao, Joao Carlos da. "Production of biodiesel by enzymatic catalysis from the castor oil: an analytical chemical study." Journal of Analytical & Pharmaceutical Research 9, no. 3 (August 7, 2020): 73–79. http://dx.doi.org/10.15406/japlr.2020.09.00355.

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The study aimed at the development of a method for obtaining biodiesel by transesterification by via methylic from castor oil using biocatalysts. Seven varieties of lipase (PPL, Candida rugosa, OS cepacea, OS cepacea immobilized on diatomaceous earth, Novozyme 435, Lipozyme and Lipozyme RM) and seven enzymatic sources from a vegetable origin (latex of the species Ficus benjamina, Manihot glaziovii Muell. Arg., Calotropis procera, Jatropha curcas L., Ficus pumila, Euphorbia tirucalli L.) were tested. Enzymatic sources of plant origin were submitted, initially, the hydrolytic activity tests to evaluate their potential as biocatalysts and, from the results obtained, two samples were selected for the experiments further synthesis of biodiesel. Validation of the method of production of biodiesel evaluated linearity, reproducibility (precision), recovery (accuracy) and the limits of detection and quantification. Among the sources of enzymes used in the synthesis of biodiesel presented the best result was the commercial enzyme Novozym 435 with 55.33% conversion yield of biodiesel in initial tests. Were conducted new tests for optimization of reactional parameters co-solvent, alcohol: oil ratio, amount of enzyme and solvent for recovery of the enzyme, which enabled a maximum yield of biodiesel to 98.84%.

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Shimotori, Yasutaka, Masayuki Hoshi, Yosuke Osawa, and Tetsuo Miyakoshi. "Synthesis of various β-D-glucopyranosyl and β-D-xylopyranosyl hydroxybenzoates and evaluation of their antioxidant activities." Heterocyclic Communications 23, no. 3 (June 27, 2017): 213–23. http://dx.doi.org/10.1515/hc-2016-0214.

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AbstractVarious β-D-glucopyranosyl and β-D-xylopyranosyl hydroxybenzoates were efficiently prepared from 2,3,4,6-tetra-O-acetyl-α-D-glucopyranosyl bromide (TAGB) or 2,3,4-tri-O-acetyl-α-D-xylopyranosyl bromide (TAXB), respectively, by amine-promoted glycosylation. Regioselective deacetylation of the resulting acetylated β-D-gluco- and β-D-xylopyranosyl hydroxybenzoates was investigated using Novozym 435 as a lipase catalyst. In the case of β-D-glucopyranosyl hydroxybenzoates, Novozym 435-catalyzed deacetylation is regioselective at C-4 and C-6 positions. On the other hand, β-D-xylopyranosyl hydroxybenzoates are deacetylated only at the C-4 position. Antioxidant activities of free hydroxybenzoic acids and the respective β-D-gluco- and β-D-xylopyranosyl hydroxybenzoates were evaluated by DPPH˙ radical scavenging as well as their inhibitory effect on autoxidation of bulk methyl linoleate. The β-D-xylopyranosyl protocatechoate, as well as quercetin and α-tochopherol, show high antioxidant activity for the radical scavenging activity by 1,1-diphenyl-2-picrylhydrazyl (DPPH˙). In bulk methyl linoleate, the antioxidant activities of β-D-gluco- and β-D-xylopyranosyl protocatechoates are higher than that of α-tocopherol.

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Senthil, Senthil Kumar, M. H. Uzir, and Z. Ahmad. "Comparative Study between Candida antarctica Lipase B and Pseudomonas floroscens as Catalyst for Polycaprolactone Production." Advanced Materials Research 626 (December 2012): 547–50. http://dx.doi.org/10.4028/www.scientific.net/amr.626.547.

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The Effects of temperature on ring-opening bulk polymerizations of ε-caprolactone was studied by using two different lipases Novozym 435 (immobilized form of lipase B from Candida antarctica), and Pseudomonas Floroscens as biocatalyst. The polymerization of ε-caprolactone was carried out at 50°C, 60°C, 70°C, 80°C, 90°C, and 100°C. For Novozym 435 the results showed that increasing the reaction time of the polymerization system resulted in an increased rate of monomer consumption and hence increased the molecular weight. For an increase in reaction time the conversion increases steadily and after a gradual increase there is a decrease which is found uniform for all the temperature showing a uniform trend. For a temperature of 70°C and 4 hours molecular weight was found to be 8.4 x 104 daltons which were the highest of all the readings that were obtained. In the copolymerizaton of ε-caprolactone (ε-CL) and δ-valerolactone using Pseudomonas fluorescens lipase at 60°C for 20 days a copolymer with molecular weight of 1.97 x 105 was obtained. Effects of the reaction time and temperature on the copolymerization have been examined.

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Kuroiwa, Takashi, Kazuyuki Kimura, Yoshihiro Aoki, Marcos A. Neves, Seigo Sato, Sukekuni Mukataka, Akihiko Kanazawa, and Sosaku Ichikawa. "Quantitative Evaluation of the Effects of Moisture Distribution on Enzyme-Induced Acylation of Trehalose in Reduced-Moisture Organic Media." Journal of Food Research 4, no. 5 (September 11, 2015): 133. http://dx.doi.org/10.5539/jfr.v4n5p133.

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Enzymatic condensation of trehalose and myristic acid in organic media (2-methyl-2-butanol and acetone) with reduced moisture content was evaluated. Monomyristoyl trehalose was synthesized using immobilized lipase B from Candida antarctica (Novozym® 435). The product yield was significantly affected by process parameters, such as the initial moisture content in organic media, as well as in immobilized enzymes, and the added concentration of molecular sieves. Up to 25% yield of monomyristoyl trehalose could be attained, depending on the process. The experimental setup used in this study consisted of a multiphase component, i.e., Novozym® 435, an organic solvent, and molecular sieves. Moisture adsorbed either onto immobilized enzymes, or molecular sieves, and free moisture content in the organic solvent were characterized using individual experiments. The relationship between process parameters and the quantitative moisture distribution in the system was also investigated. The results presented in this paper indicates that a process design considering moisture distribution in the reaction system is important for understanding the effect of moisture on the reaction as well as for optimizing the process parameters.

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Hrčková, M., M. Rusňáková, and J. Zemanovič. "Enzymatic hydrolysis of defatted soy flour by three different proteases and their effect on the functional properties of resulting protein hydrolysates." Czech Journal of Food Sciences 20, No. 1 (November 18, 2011): 7–14. http://dx.doi.org/10.17221/3503-cjfs.

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Commercial defatted soy flour (DSF) was dispersed in distilled water at pH 7 to prepare 5% aqueous dispersion. Soy protein hydrolysates (SPH) were obtained by enzymatic hydrolysis of the DSF using three different proteases (Flavourzyme 1000 L, No-vozym FM 2.0 L and Alcalase 2.4 L FG). The highest degree of hydrolysis (DH 39.5) was observed in the presence of protease Flavourzyme. SPH were used for measuring functional properties (foaming stability, gelation). Treatment with Flavourzyme improved foaming of proteins of DSF. Foaming stability was low in the presence of Novozym. Proteases treated DSF showed good gelation properties, mainly in the case of treatment with Flavourzyme. SDS-PAGE analysis showed that after enzyme ad-dition to the 5% aqueous dispersion of DSF each enzyme degraded both b-conglycinin and glycinin. In general, the basic polypeptide from glycinin showed the highest resistance to proteolytic activity. The most abundant free amino acids in the hydrolysates were histidine (30%), leucine (24%) and tyrosine (19%) in the case of the treatment with proteases Alcalase and Novozym, and arginine (22.1%), leucine (10.6%) and phenylalanine (12.9%) in the case of the treatment with Flavourzyme.  

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Tang, Feng Xiang, Yun Bo Li, Chun Meng, and Xue Qing Zhao. "A Two-Step Resolution for Preparing Enantiopure (S)-Ethyl Nipecotate." Advanced Materials Research 393-395 (November 2011): 559–66. http://dx.doi.org/10.4028/www.scientific.net/amr.393-395.559.

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Enantiopure nipecotic acid or ethyl nipecotate are key precursors for synthesizing a variety of pharmaceutically important compounds. In this work a two-step resolution of racemic ethyl nipecotate was developed to prepare enantiopure (S)-ethyl nipecotate. In the enzymatic resolution step, six lipases were screened for their ability to enantioselectively hydrolyze rac-ethyl nipecotate in t-butanol at 30°C and Novozym 435 was found to be the most effective. Solvent effects on the hydrolysis conversion and enantioselectivity showed that water was the optimum medium. When rac-ethyl nipecotate concentration was kept at 0.5M, the hydrolysis under optimum conditions (lipase loading 5mg/mL, phosphate buffer pH 7.0, reaction temperature 30°C, reaction time 6h) afforded 68.9% ees and 69.5% eep at 49.8% conversion. Novozym 435 preferentially hydrolyzed (R)-ethyl nipecotate over (S)-enantiomer. A parallel reaction model was suggested and found to fit the experimental initial rate data very well. (S)-enriched ethyl nipecotate was further resolved using (D)-tartaric acid and enantiopure (S)-ethyl nipecotate (98.5% ee) was acquired in 84.3% yield. The overall yield of enantiopure (S)-ethyl nipecotate by this two-step resolution was up to 36.0%.

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Salimon, Jumat, Nadia Salih, and Bashar Mudhaffar Abdullah. "Production of Chemoenzymatic Catalyzed Monoepoxide Biolubricant: Optimization and Physicochemical Characteristics." Journal of Biomedicine and Biotechnology 2012 (2012): 1–11. http://dx.doi.org/10.1155/2012/693848.

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Linoleic acid (LA) is converted to per-carboxylic acid catalyzed by an immobilized lipase fromCandida antarctica(Novozym 435). This per-carboxylic acid is only intermediate and epoxidized itself in good yields and almost without consecutive reactions. Monoepoxide linoleic acid 9(12)-10(13)-monoepoxy 12(9)-octadecanoic acid (MEOA) was optimized using D-optimal design. At optimum conditions, higher yield% (82.14) and medium oxirane oxygen content (OOC) (4.91%) of MEOA were predicted at 15 μL of H2O2, 120 mg of Novozym 435, and 7 h of reaction time. In order to develop better-quality biolubricants, pour point (PP), flash point (FP), viscosity index (VI), and oxidative stability (OT) were determined for LA and MEOA. The results showed that MEOA exhibited good low-temperature behavior with PP of−41°C. FP of MEOA increased to128°Ccomparing with115°Cof LA. In a similar fashion, VI for LA was 224 generally several hundred centistokes (cSt) more viscous than MEOA 130.8. The ability of a substance to resist oxidative degradation is another important property for biolubricants. Therefore, LA and MEOA were screened to measure their OT which was observed at 189 and168°C, respectively.

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Yan, Zijun, Xin Zhang, Zuoao Wu, Kaiqun Wu, and Yuliang Wang. "Enzymatic Synthesis of Glycerol Monolaurate Catalyzed by Lipase Novozym 435." University Chemistry 35, no. 4 (2020): 119–24. http://dx.doi.org/10.3866/pku.dxhx201911062.

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Yasmin, Tahmina, Tao Jiang, Buxing Han, Jicheng Zhang, and Xiumin Ma. "Transesterification reaction catalysed by Novozym 435 in supercritical carbon dioxide." Journal of Molecular Catalysis B: Enzymatic 41, no. 1-2 (July 2006): 27–31. http://dx.doi.org/10.1016/j.molcatb.2006.04.001.

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FENG, Jun. "NOVOZYM-435 CATALYZED RING-OPENING POLYMERIZATION OF A MACROCYCLIC CARBONATE." Acta Polymerica Sinica 008, no. 7 (September 15, 2008): 686–90. http://dx.doi.org/10.3724/sp.j.1105.2008.00686.

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Journal articles on the topic 'Novozym'

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