Enzymatic glyceride synthesis in a foam reactor

We report the results of our study on Rhizomucor miehei lipaseâ catalyzed lauric acidâ glycerol esterification in a foam reactor. A satisfactory yield of glyceride synthesis can be achieved with an unusually high initial water content (50% w/w). We found that product formation could be regulated by controlling foaming. Foaming was a function of the air flow rate, reaction temperature, pH value, ionic strength, and substrate molar ratio. Monolaurin and dilaurin, which constituted nearly 80% of the total yield, were the two dominant products in this reaction; trilaurin was also formed at the initial stages of the reaction. A study of pH and ionic strength effects on an independent basis revealed that they affect the interfacial mechanism in different manners. On varying the ratio of lauric acid and glycerol, only a slight change in the degree of conversion was detected and the consumption rate of fatty acid was approximately the same.Peer Reviewedhttps://deepblue.lib.umich.edu/bitstream/2027.42/141443/1/aocs0643.pd

Enzymatic synthesis of low-trans blends from fractionated mustard oil and palm stearin with linoleic acid by response surface methodology

Low-trans blend (LTB) was produced from the fractionated mustard oil (solid phase, S-MO) and palm stearin (PS) through lipase-catalyzed reaction, in which linoleic acid (LA) was intentionally incorporated. For optimizing the reaction condition, response surface methodology (RSM) was employed with three reaction variables such as substrate mole ratio of S-MO to PS (Xsub1), reaction temperature (Xsub2) and reaction time (Xsub3). The predictive models were adequate and reproducible due to no significant lack of fit and the P-value of the model was very small ω6/ω3 ratio, and satisfactory level of coefficient of determination (R2 = 0.89) for ω6/ω3 ratio. The ω6/ω3 ratio of LTB was affected by substrate mole ratio and reaction temperature but reaction time had no significant effect. For considering the ω6/ω3 ratio, the optimum condition found 1:1.7 substrate mole ratio, 61.42 reaction temperature and 25.85 h reaction time

Enzymatic approach to biodiesel production

The need for alternative energy sources that combine environmental friendliness with biodegradability, low toxicity, renewability, and less dependence on petroleum products has never been greater. One such energy source is referred to as biodiesel. This can be produced from vegetable oils, animal fats, microalgal oils, waste products of vegetable oil refinery or animal rendering, and used frying oils. Chemically, they are known as monoalkyl esters of fatty acids. The conventional method for producing biodiesel involves acid and base catalysts to form fatty acid alkyl esters. Downstream processing costs and environmental problems associated with biodiesel production and byproducts recovery have led to the search for alternative production methods and alternative substrates. Enzymatic reactions involving lipases can be an excellent alternative to produce biodiesel through a process commonly referred to alcoholysis, a form of transesterification reaction, or through an interesterification (ester interchange) reaction. Protein engineering can be useful in improving the catalytic efficiency of lipases as biocatalysts for biodiesel production. The use of recombinant DNA technology to produce large quantities of lipases, and the use of immobilized lipases and immobilized whole cells, may lower the overall cost, while presenting less downstream processing problems, to biodiesel production. In addition, the enzymatic approach is environmentally friendly, considered a "green reaction", and needs to be explored for industrial production of biodiesel

Biocatalysis for the Production of Industrial Products and Functional Foods from Rice and Other Agricultural Produce

Many industrial products and functional foods can be obtained from cheap and renewable raw agricultural materials. For example, starch can be converted to bioethanol as biofuel to reduce the current demand for petroleum or fossil fuel energy. On the other hand, starch can also be converted to useful functional ingredients, such as high fructose and high maltose syrups, wine, glucose, and trehalose. The conversion process involves fermentation by microorganisms and use of biocatalysts such as hydrolases of the amylase superfamily. Amylases catalyze the process of liquefaction and saccharification of starch. It is possible to perform complete hydrolysis of starch by using the fusion product of both linear and debranching thermostable enzymes. This will result in saving energy otherwise needed for cooling before the next enzyme can act on the substrate, if a sequential process is utilized. Recombinant enzyme technology, protein engineering, and enzyme immobilization are powerful tools available to enhance the activity of enzymes, lower the cost of enzyme through large scale production in a heterologous host, increase their thermostability, improve pH stability, enhance their productivity, and hence making it competitive with the chemical processes involved in starch hydrolysis and conversions. This review emphasizes the potential of using biocatalysis for the production of useful industrial products and functional foods from cheap agricultural produce and transgenic plants. Rice was selected as a typical example to illustrate many applications of biocatalysis in converting low-value agricultural produce to high-value commercial food and industrial products. The greatest advantages of using enzymes for food processing and for industrial production of biobased products are their environmental friendliness and consumer acceptance as being a natural process