Lipase-Catalyzed Biochemical Reactions in Novel Media: A Review

Patel, Mayank T.; Nagarajan, Ramaswamy; Kilara, Arun

doi:10.1080/00986449608936574

Cited by 27 publications

(29 citation statements)

References 181 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Since the beginning of the 20th century, it has been known that lipases (2)(3)(4) also can catalyze the hydrolysis of fats (5). Fat splitting, with lipase as a catalyst, is advantageous compared to a conventional process due to low energy consumption, high product quality (1,6), and greater safety.…”

mentioning

confidence: 99%

Parameter optimization for the enzymatic hydrolysis of sunflower oil in high‐pressure reactors

Primožič

Habulin

Knez

2003

J Americ Oil Chem Soc

View full text Add to dashboard Cite

This study is concerned with the hydrolysis of sunflower oil in the presence of lipase preparation Lipolase 100T (Aspergillus niger lipase). Supercritical carbon dioxide was used as a solvent for this reaction. In a high-pressure stirred tank reactor operated in a batch mode, the effects of various process parameters (temperature, pressure, enzyme/substrate ratio, pH, and oil/buffer ratio) were investigated to determine the optimal reaction rate and conversion for the hydrolysis process. The optimal concentration of lipase was 0.0714 g/mL of CO 2 -free reaction mixture, and the highest conversions of oleic acid (0.193 g/g of oil phase) and linoleic acid (0.586 g/g of oil phase) were obtained at 50°C, 200 bar, pH = 7, and an oil/buffer ratio of 1:1 (w/w).

show abstract

mentioning

confidence: 99%

Parameter optimization for the enzymatic hydrolysis of sunflower oil in high‐pressure reactors

Primožič

Habulin

Knez

2003

J Americ Oil Chem Soc

View full text Add to dashboard Cite

show abstract

“…Widespread applications of lipase-catalyzed reactions in organic media for the food, pharmaceutical, and olechemical industries are believed to exist (1)(2)(3)(4). The fundamental advantage of reaction selectivity favors the use of lipases over chemical processes for transforming acylglycerols into value-added specialty products, commonly referred to as structured lipids (5,6).…”

mentioning

confidence: 99%

FA selectivity of lipases in acyl‐transfer reactions with acetate esters of polyols in organic media

Lee

Parkin

2003

J Americ Oil Chem Soc

View full text Add to dashboard Cite

FA reaction selectivity of Burkholderia cepacia, Rhizomucor miehei, and Candida antarctica fraction B lipases was compared between acyl-transfer and esterification reactions. Multicompetitive reaction mixtures containing a series of n-chain FA (a C 4 -C 18 series; and a C 18:X series, where X = 0-3 double bonds) and a single acetate ester co-substrate [triacetin, 1,2-propanediol (1,2-PD) diacetate, and 1,3-PD diacetate] were studied in tert-butyl methyl ether at an a w of 0.69. For B. cepacia lipase, FA optima for C 8 , C 16 , and C 18:2 were observed in all reactions with 1.0-to 5.9-fold differences in FA selectivity. For R. miehei lipase, an optimum for C 8 FA was observed in all reactions with 1.2-to 6.7-fold differences in FA selectivity. For C. antarctica lipase, FA optima for C 8 /C 10 were observed in all reactions with 1.0-to 2.8-fold differences in FA selectivity. FA selectivities were broadly modulated upon changing from free polyol to acetate ester co-substrates for B. cepacia and R. miehei lipases, whereas FA selectivity modulations were more specific upon this change in reaction configuration for C. antarctica B lipase. For all lipases, reactivity toward unsaturated C 18:X FA was enhanced in acyl-transfer relative to esterification reactions with these polyol co-substrates. FIG. 3. α-Values for FA in acyl-transfer reactions catalyzed by Candida antarctica lipase B with (A) triacetin, (B) 1,2-PD diacetate, or (C) 1,3-PD diacetate. The legend is the same as for Figure 1, except that lipase was used at levels of 25 to 30 mg for esterification and 50 to 300 mg for acyl-transfer. Results are expressed as means from two or three experiments with a CV of about 5%. For abbreviations see Figure 1.

show abstract

“…They can catalyse reactions of insoluble substrates at the lipid-water interface, preserving their catalytic activity in organic solvents [3]. This makes of lipases powerful tools for catalysing not only hydrolysis, but also various reverse reactions such as esterification, transesterification, aminolysis, or thiotransesterifications in anhydrous organic solvents [4, 5].…”

Section: Lipases For Applied Biocatalysismentioning

confidence: 99%