Triacylhydrolase Research Paper

Lipase (triacylglycerol acylhydrolase E.C.3.1.1.3) is a class of enzymes belonging to the serine hydrolases and widely known as important biocatalyst which involved in hydrolysis, interesterification, esterification, alcoholysis, acidolysis and aminolysis (Rajendran et al., 2009). These industrial potential enzymes are ubiquitous in nature and produced by various organisms including animal, plant, bacteria, fungi and yeast (Wu et al. 1995). However, lipases derived from bacterial are the most versatile enzymes and commercially applied in various industries (Chouchan and Dawande, 2010). Recently, the number of research and publication related to the properties and industrial applications of lipase-catalyzed reaction increased rapidly and received

Gailapati and Banerjee (2013) reported that immobilized lipase was employed for transesterification under solvent-free condition to produce flavor esters such as methyl butyrate and actyl acetate with the characteristic of pineapple and orange respectively. Lipase also has been utilized in the dairy industry to develop characteristic flavor of cheese and also involved in the hydrolysis of milk fat (Rajendran et al., 2009). It was also used as lubricant and additives in cosmetic and as drug formulation in the pharmaceutical industry. Lipase plays an important role in paper industry to remove the pitch from pulp and also involved in the removal of subcutaneous fat in leather industry. Nowadays, the application of lipase as biocatalyst for biodiesel synthesis also increased rapidly. Immobilized Enterobacter aeruginenes lipase was used for the transesterification of Jatropa oil in t. butanol solvent for the production of biodiesel with the maximum yield of 94% (Kumari et al. 2009). Lipase was also reported in the production of biodiesel by transesterification of vegetable oil such as sunflower oil and soybean oil (Leca et al. 2010). Usmani and patil (2010) studied the lipase catalysed interesterrification of Neem, Karanja and rice bran oil for the production of

Researchers found that microgravity condition provide better conditions for growing high quality protein crystals with better internal orders (Aris et al., 2014). Crystallization in microgravity environments improved the size and interface of protein crystals (Rahman et al.2010). These high quality protein crystals are essential to determine their structure via diffraction analysis. The improvement of protein crystals lead to a better understanding of the structural mechanism and their biological activity for the production of high quality enzymes. Hence, molecular modeling programs and site-directed mutagenesis can be applied to manipulate the structure of