University of Calcutta (informally known as Calcutta University or CU) is a collegiate public state university located in Kolkata, West Bengal, India.&nbsp;Within India it is recognized as a &quot;Five-Star University&quot; and accredited &quot;A&quot; Grade by National Assessment and Accreditation Council.

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The University of Calcutta has secured the Fifth position among the Universities of India in the prestigious &quot;Indian University Ranking 2019&quot; list, released by the NIRF of the Ministry of Human Resource Development, Government of India.

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It was established on 24 January 1857, and was one of the first institutions in Asia to be established as a multidisciplinary and Western-style university. Its alumni and faculty include several heads of state, heads of government, social reformers, prominent artists, only academy award winner and Dirac medal winner in India, many Fellows of the Royal Society and five Nobel laureates as of 2019 which is highest in South Asia.

University Of Calcutta

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Chemical Engineering

Colloids and Surfaces B: Biointerfaces

Mixed micelles and bicontinuous microemulsions: Promising media for enzymatic reactions

This work studied hydrolysis of castor oil to ricinoleic acid, catalyzed by immobilized porcine pancreas lipase (PPL) and impact of surfactant on its augmentation. In immobilization of lipase through entrapment in calcium alginate beads, concentration of calcium chloride (CaCl2) was the most significant factor. Optimum conditions for immobilization were, 1.3 M CaCl2 and 12% (w/v) sodium alginate. On cross-linking with glutaraldehyde after entrapment in calcium alginate bead, PPL led to 2.7-fold higher hydrolysis compared to only entrapped PPL. Most suitable surfactant and speed of agitation were Span 80 and 300 rpm, respectively, in enhancing ricinoleic acid production involving cross-linked and entrapped PPL. Central composite design and subsequent optimization with response surface methodology (RSM) found optimum production (recovery) as 21.2% (in 3 h and 25 °C) under the optimum set of process conditions like 9.96 mg lipase/ml, pH of 8.8, 0.014 M Span 80, 2.98% (v/v) glutaraldehyde, 1.3 M CaCl2 and 12% (w/v) sodium alginate. Each of concentration of lipase, pH, surfactant (Span 80) concentration and glutaraldehyde concentration was found to be highly significant. Interactions between any two of these four variables remained insignificant. On varying temperature keeping other variables at their optima, maximum recovery for free lipase (31.29% in 3 h) was obtained at 35 °C; whereas, for immobilized lipase, recovery was maximum (26.27% in 3 h) at 45 °C. Immobilized lipase acted much better than free lipase at higher temperatures. © 2020 Taylor & Francis Group, LLC.

Journal of Dispersion Science and Technology

Surfactant assisted production of ricinoleic acid using cross-linked and entrapped porcine pancreas lipase

Lipase can catalyze varieties of reactions at the interface of aqueous and organic phase. Among various alternatives to modify catalytic performance of lipase, the addition of surfactants, particularly nonionic surfactants, has been widely studied. Low concentrations of nonionic surfactants augment lipase catalysis; on increasing surfactant concentration, often the catalytic performance decreases. Mole ratio of water to (nonionic) surfactant also has a profound effect on lipase activity. Catalytic abilities of some lipases are either enhanced or reduced in the presence of all nonionic surfactants of the same type, whereas for some other lipases, nonionic surfactants of the same type have mixed effect. Nonionic surfactant even changes substrate specificity of lipase. Water-in-ionic liquid microemulsion involving nonionic surfactant often performs better than other systems in improving catalytic ability of lipase. Tween and Triton surfactants often enhance enantiomeric separation catalyzed by lipase. Nonionic surfactants significantly affect activities of immobilized lipase, being present either as a component during immobilization or as a component in reaction medium. Lipases coated with nonionic surfactants act better than reverse micelles and microemulsions containing lipase. Thus, nonionic surfactants help lipase catalyzed processes in various media to enhance production of useful compounds like flavor ester, structured lipids, optically pure compounds, and noncrystalline polymers. © 2019, Springer Science+Business Media, LLC, part of Springer Nature.

Applied Biochemistry and Biotechnology

Lipase Catalysis in Presence of Nonionic Surfactants

In present study involving castor oil hydrolysis catalyzed by porcine pancreas lipase, organic solvent, and ionic liquid were applied to augment production of ricinoleic acid. Toluene was the best organic solvent (30.18% hydrolysis in 2 h). In presence of 1-butyl-3-methylimidazolium hexafluorophosphate ([BMIM][PF6]), an ionic liquid, the optimal conditions were, 0.12 g ionic liquid/g oil, 4 mg enzyme/g oil, 2 g buffer/g oil, pH of 8, and 2.5 h. Under this condition, ricinoleic acid recovery was 43.41 and 52% at 25 °C and 35 °C, respectively. Organic solvent concentration, enzyme concentration, buffer concentration and time had significant impacts on lipase catalyzed hydrolysis in the presence of organic liquid; whereas, pH and speed remained insignificant. In hydrolysis involving ionic liquid, time had most important effect on ricinoleic acid production. Interaction between enzyme and buffer concentration was most significant. Interactions of ionic liquid concentration with all other variables were also significant besides buffer concentration–time interaction. © 2019, © 2019 Taylor & Francis Group, LLC.

GENERAL

Chemical Engineering Communications

Biocatalytic production of ricinoleic acid from castor oil: augmentation by ionic liquid

Current Biochemical Engineering

Lipase Catalyzed Modification of Mustard Oil: A Review

Lipase is an enzyme which catalyzes hydrolysis, esterification and transesterification processes. Type (origin) of lipase affects process conditions and final conversion. Use of these biocatalytic properties of lipase in modification of various vegetable oils is depicted in different patents, leading to varieties of beneficial products. Production and concentration of polyunsaturated fatty acids like eicosapentanoic acid, docosapentanoic acid and docosahexanoic acid were carried out through lipase catalyzed hydrolysis. Hydrolysis followed by reesterification was also employed in some patents to concentrate long chain polyunsaturated fatty acids in triacylglycerol fraction or free fatty acid fraction as per specific requirements. Ethanolysis of fish oil hexyl esters was also described in some studies to concentrate similar fatty acids. Combined ethanolysis and esterification, ethanolysis and transesterification were also conducted in some patents to concentrate these desirable fatty acids. Degumming using phospholipase and biodiesel production with lipase as catalyst were also carried out leading to some notable patents. Reactor configuration for maximizing conversion was also patented. Removal of diacylglycerols from their mixture with triacylglycerols led to specifically designed triacylglycerol mixture for catering certain purposes. © 2013 Bentham Science Publishers.

Recent Patents on Engineering

Recent patents on lipase catalyzed vegetable and fish oil modification

Lipase (triacylglycerol acylhydrolase) is a unique enzyme which can catalyze various types of reactions such as hydrolysis, esterification, alcoholysis etc. In particular, hydrolysis of vegetable oil with lipase as a catalyst is widely studied. Free lipase, lipase immobilized on suitable support, lipase encapsulated in a reverse micelle and lipase immobilized on a suitable membrane to be used in membrane reactor are the most common ways of employing lipase in oil hydrolysis. Castor oil is a unique vegetable oil as it contains high amounts (90%) of a hydroxy monounsaturated fatty acid named ricinoleic acid. This industrially important acid can be obtained by hydrolysis of castor oil. Different conventional hydrolysis processes have certain disadvantages which can be avoided by a lipase-catalyzed process. The degree of hydrolysis varies widely for different lipases depending on the operating range of process variables such as temperature, pH and enzyme loading. Immobilization of lipase on a suitable support can enhance hydrolysis by suppressing thermal inactivation and estolide formation. The presence of metal ions also affects lipase-catalyzed hydrolysis of castor oil. Even a particular ion has different effects on the activity of different lipases. Hydrophobic organic solvents perform better than hydrophilic solvents during the reaction. Sonication considerably increases hydrolysis in case of lipolase. The effects of additives on the same lipase vary with their types. Nonionic surfactants enhance hydrolysis whereas cationic and anionic surfactants decrease it. A single variable optimization method is used to obtain optimum conditions. In order to eliminate its disadvantages, a statistical optimization method is used in recent studies. Statistical optimization shows that interactions between any two of the following pH, enzyme concentration and buffer concentration become significant in presence of a nonionic surfactant named Span 80. © 2013 Informa Healthcare USA, Inc.

Critical Reviews in Biotechnology

Lipase applications in oil hydrolysis with a case study on castor oil: A review

In this study, response surface methodology was applied to maximize production of erucic acid from lipase catalyzed mustard oil hydrolysis. Regioselective porcine pancreas lipase was used as catalyst. A quadratic model was developed by applying 2 4 full factorial central composite design. The optimal conditions obtained on numerical optimization of this model were; temperature 24.2°C, pH 8.70, enzyme concentration 2.71mg/g oil and buffer concentration 1.25g/g oil. Maximum response, i.e., 'percentage of total erucic acid formed' was 95.5% in 6h, much better than the conversion obtained by earlier single variable optimization method. The two most significant variables were pH and buffer concentration. Interaction between temperature and buffer concentration also had significant effect. © 2011 Elsevier B.V..

Chemical Engineering Journal

Optimal hydrolysis of mustard oil to erucic acid: A biocatalytic approach

Selective hydrolysis of brown mustard oil (from Brassica juncea) with regioselective porcine pancreas lipase was studied in this work. Buffer and oil phase were considered as the continuous and dispersed phases, respectively. Effects of speed of agitation, pH of the buffer phase, temperature, buffer-oil ratio and enzyme concentration on hydrolysis were observed. The best combination of process variables was: 900 rpm, pH 9, 35°C, buffer-oil ratio of 1:1 and enzyme concentration of 10 mg/g oil. These standard conditions led to 50% hydrolysis and selective production of 55% erucic acid in 6 h. Cations like Mg 2+ and Ca 2+ increased hydrolysis, but Cu 2+ strongly inhibited it. Organic solvents decreased hydrolysis, though the decrease was minimum for isooctane. A mixed surfactant comprising of Span 80 and Tween 80 increased erucic acid production by 57% at a buffer-oil ratio of 0.2:1.

Fulltext

Brazilian Journal of Chemical Engineering

Effects of process variables and additives on mustard oil hydrolysis by porcine pancreas lipase

Application of mixed surfactants coupled with statistical optimization in lipase catalyzed oil hydrolysis is presented for the first time in this study. Selective hydrolysis of brown mustard oil to erucic acid by porcine pancreas lipase was enhanced by mixed surfactants comprising of an oil-soluble nonionic surfactant (Span 80) and a watersoluble nonionic surfactant (Tween 80). The production of erucic acid was maximized using statistically designed experiments and subsequent analysis of their result by response surface methodology. The most significant variables were enzyme concentration and concentration of Tween 80. Small changes in pH and concentration of Span 80 also produced a significant change in the production of erucic acid. Temperature and speed of agitation were insignificant variables and were fixed at 35oC and 900 rpm, respectively. Under these conditions, the optimal combination of other variables were pH 9.65, 2.13 mg/g enzyme in oil, 9.8 × 10-3 M Span 80 (in oil), and 4 × 10-3 M Tween 80 (in buffer). These conditions led to formation of 99.69% of the total erucic acid in 1.25 h. Interaction of enzyme concentration with pH significantly affected erucic acid production. © 2011 The Korean Society for Biotechnology and Bioengineering and Springer-Verlag Berlin Heidelberg.

Biotechnology and Bioprocess Engineering

Erucic acid production using porcine pancreas lipase: Enhancement by mixed surfactants

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 24 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. © 2009 Elsevier Ltd. All rights reserved.

Bioresource Technology

Surfactant enhanced ricinoleic acid production using Candida rugosa lipase

IIT Kharagpur

Surfactant Enhanced Lipase Catalyzed Oil Hydrolysis

In this study, castor oil is hydrolyzed in presence of Candida rugosa lipase, while in the buffer (aqueous) phase as a dispersion medium. The following conditions were used to optimize the process: speed of agitation, initial pH of buffer phase, temperature, and ratio of buffer phase volume to oil weight. The optimal conditions are 1,100 rpm, pH 6.5, temperature 35°C, and 3:1 buffer phase volume to oil weight ratio. Under these described conditions, the reusability of lipase was tested and it was found that nearly 80% of original hydrolysis percentage was achieved after the first recycle. © The Korean Society for Biotechnology and Bioengineering and Springer-Verlag Berlin Heidelberg GmbH 2009.

Optimization of process variables in castor oil hydrolysis by Candida rugosa lipase with buffer as dispersion medium

In this study, response surface methodology was applied to optimize process variables like temperature, pH, enzyme concentration (mg/g oil), and buffer concentration (g/g oil) for hydrolysis of castor oil using Candida rugosa lipase. A 24 full factorial central composite design was used to develop the quadratic model that was subsequently optimized and the optimal conditions were as follows: temperature 40 °C, pH 7.72, enzyme concentration 5.28 mg/g oil, buffer concentration 1 g/g oil and there was 65.5% conversion in 6 h. These predicted optimal conditions agreed well with the experimental results. This is the first report on the application of response surface methodology in castor oil hydrolysis using C. rugosa lipase with higher percentage conversion in 6 h. © 2008 Elsevier Ltd. All rights reserved.