Ricinoleic Acid Production Research Articles

Surfactant enhanced ricinoleic acid production using Candida rugosa lipase

In this study, ricinoleic acid was produced on surfactant enhanced castor oil hydrolysis using Candida rugosa lipase. The most effective surfactant was Span 80. Employing fractional factorial design, the most suitable temperature and surfactant concentration were found to be 31 °C and 0.257% (w/w in buffer) respectively whereas pH, enzyme concentration, buffer concentration and agitation were identified as the most significant independent variables. A 2 4 full factorial central composite design was applied and the optimal conditions were found to be pH 7.0, enzyme concentration 7.42 mg/g oil, buffer concentration 0.20 g/g oil and agitation 1400 rpm with the maximum response of 76% in 4 h. The most important variable was pH, whereas enzyme and buffer concentrations also showed pronounced effect on response. This is the first report on the application of response surface methodology for optimizing surfactant enhanced ricinoleic acid production using C. rugosa lipase.

Production of Ricinoleic Acid from Castor Oil by Immobilised Lipases

Porcine pancreatic lipase (PPL), Candida rugosa lipase (CRL), and Castor bean lipase (CBL) were immobilized on celite by deposition from aqueous solution by the addition of hexane. Lipolytic performance of free and immobilized lipases were compared and optimizations of lipolytic enzymatic reactions conditions were performed by free and immobilized derivatives using olive oil as substrate. Afterwards, the influence on lipolysis of castor oil of free lipases and immobilized lipase derivatives have been studied in the case of production of ricinoleic acid. All of the lipases performances were compared and enzyme derivative was selected to be very effective on the production of ricinoleic acid by lipolysis reaction. Various reaction parameters affecting the production of ricinoleic acid were investigated with selected the enzyme derivative. The maximum ricinoleic acid yield was observed at pH 7–8, 50°C, for 3 hours of reaction period with immobilized 1,3-specific PPL on celite. The kinetic constants Km and Vmax were calculated as 1.6 × 10−4 mM and 22.2 mM from a Lineweaver–Burk plot with the same enzyme derivative. To investigate the operational stability of the lipase, the three step lipolysis process was repeated by transferring the immobilized lipase to a substrate mixture. As a result, the percentange of conversion after usage decreased markedly.

Selective Production of Ricinoleic Acid by Hydrolysis of Castor Oil using Lipase Immobilized in N-polyisopropylacrylamide Gel.

Candida cylindracea起源のリパーゼあるいはRhizopus起源のリパーゼをN-イソプロピルアクリルアミド, N, N'メチレンビスアクリルアミド, アクリルアミドの共重合によって得られるゲルビーズ中に包括固定化した.固定化リパーゼと遊離リパーゼを用いて, ヒマシ油の加水分解を37℃で行い, 固定化の最適条件及び, リシノール酸の選択的生成について検討した. その結果, リパーゼをN-ポリイソアクリルアミドゲル中に包括固定化することにより遊離リパーゼと比較して, 副生成物であるエストライドの生成が抑制され, リシノール酸の生成率と酵素の熱安定性が増大した.