Microbial lipase

Lipase (Microbial) Activity for Medium- and Long-Chain Fatty Acids. .. 914... 

LIPASE (MICROBIAL) ACTIVITY FOR MEDIUM- AND LONG-CHAIN FATTY ACIDS... 

Lipase (Microbial) Activity for Medium- and Long-Chain Fatty Acids, (S3)105 Lysozyme Activity, (S3)106 Maltogenic Amylase Activity, 804 Milk-Clotting Activity, 805 Pancreatin Activity, 805 Pepsin Activity, 807 Phospholipase A2 Activity, 808 Phytase Activity, 808 Plant Proteolytic Activity, 810 Proteolytic Activity, Bacterial (PC), 811 Proteolytic Activity, Fungal (HUT), 812 Proteolytic Activity, Fungal (SAP), 813 Pullulanase Activity, 814 Trypsin Activity, 814 Enzyme Assays, 786 Enzyme-Hydrolyzed (Source) Protein,... 

Keywords Enantiopure epoxides. Oxidative enzymes. Cytochrome P-450, co-hydroxylases. Methane monooxygenases. Lipases, Microbial oxidations. Epoxide hydrolases. Biotransformations. 

The enzymes used for modification of oils and fats are extraoelluar microbial lipases. They are excreted by micro-organisms into the growth medium to catalyse the degradation of lipids, and can be produced on a large scale by fermentation. 

Persson, M., Costes, D., Wehtje, E. and Adlercreutz, P. (2002) Effects of solvent, water activity and temperature on lipase and hydroxynitrile lyase enantioselectivity. Enzyme and Microbial Technology, 30, 916-923. 

Mitsuda S, Umemura T, Hirohara H (1988) Preparation of an optically pure secondary alcohol of synthetic pyrethroids using microbial lipases. Appl Microbiol Biotechnol 29 310-315... 

E. Rogalska, C. Cudrey, F. Ferrato, R. Verger, Stereoselective Hydrolysis of Triglycerides by Animal and Microbial Lipases , Chirality 1993, 5, 24-30. 

Schmid, R.D. and Verger, R., Lipases interfacial enzymes with attractive applications. Angew. Chem. Int. Ed., 1998, 37, 1608-1633 Hasan, F., Shah, A.A. and Hameed, A., Industrial applications of microbial lipases. Enzyme. Microb. TechnoL, 2006, 39, 235-251. 

The greatest variety of industrial enzymes are presently derived from microbial sources, with a lesser diversity coming from plant and animal sources 34), Enzymes derived from plant sources and which are used extensively in the food industry include papain, bromelain, ficin, and amylases. Animal enzymes of economic importance include trypsins, lipases, and gastric proteases. 

Endogenous microbial enzymes are sometimes utilized to break down their parent cells, and thus extract valuable intracellular materials. For instance, in the production of yeast extract, cells are allowed to autolyse at about pH 5 and 55 0. Proteases are probably the most important class of enzymes involved in autolysis, although others such as glucanases, lipases and nucleases also have... 

The stability of the ester surfactants against enzymatic hydrolysis by two different microbial Upases, Mucor miehei lipase (MML) and Candida antarc-tica lipase B (CALB) added separately to the surfactant solutions, was also investigated, see Fig. 5 [19]. It is obvious that hydrolysis of the unsubstituted surfactant is much faster with both CALB and MML than that of the substituted surfactants, i.e., increased steric hindrance near the ester bond leads to decreased hydrolysis rate. Since the specificity of the enzyme against its substrate is determined by the structure of the active site, it can be concluded, as expected, that the straight chain surfactant most easily fits into the active site of both enzymes. 

Balcao, V.M., Paiva, A.L. and Malcata, F.X. (1996) Bioreactors with immobilized lipases State of the art. Enzyme and Microbial Technology, 18, 392-416. 

Bouwer, S.T., Cuperms, F.P. and Derksen, J.T.P. (1997) The performance of enzyme-membrane reactors with immobilized lipase. Enzyme and Microbial Technology, 21, 291-296. 

Lipases play an important role in organic synthesis and also in flavour biotechnology. Pig pancreatic extract and especially many microbial lipases are used for ester hydrolysis, esterification (alcohol and acid), transesterification (ester and... 

The resolution of the commercially available racemic frans-jasmonate to (-)-fraMS-jasmonate by microbial lipase has been described by Serra et al. [22]. 

The biotechnological synthesis of lactones has reached a high standard. Besides microbial production, lactones can also be enzymatically produced. For instance, a lipase-catalysed intramolecular transesterification of 4-hydroxy-carboxylic esters leads enantioselectively (ee>80%) to (S)-y-lactones the chain length may vary from C5 to Cl 1 [13]. y-Butyrolactone can be produced in that way with lipase from Mucor miehei [30]. 

Fig. 23.1 Microbial routes from natural raw materials to and between natural flavour compounds (solid arrows). Natural raw materials are depicted within the ellipse. Raw material fractions are derived from their natural sources by conventional means, such as extraction and hydrolysis (dotted arrows). De novo indicates flavour compounds which arise from microbial cultures by de novo biosynthesis (e.g. on glucose or other carbon sources) and not by biotransformation of an externally added precursor. It should be noted that there are many more flavour compounds accessible by biocatalysis using free enzymes which are not described in this chapter, especially flavour esters by esterification of natural alcohols (e.g. aliphatic or terpene alcohols) with natural acids by free lipases. For the sake of completeness, the C6 aldehydes are also shown although only the formation of the corresponding alcohols involves microbial cells as catalysts. The list of flavour compounds shown is not intended to be all-embracing but focuses on the examples discussed in this chapter... 

Lipases, which are noted for their tolerance of organic solvents, were obvious candidates for biocatalysis in ionic liquids. Indeed, stable microbial lipases, such as CaLB [8, 54, 55, 56] and Pseudomonas cepacia lipase (PcL) [28, 55, 57] were cat-alytically active in the ionic liquids of the l-alkyl-3-methylimidazolium and 1-alkylpyridinium families, in combination with anions such as [BF4], [PF6], [TfO] and [ Tf2N]. Early results were not always consistent, which may be caused by impurities that result from the preparation of the ionic liquid. Lipase-mediated transesterification reactions (Figure 10.3) in these ionic liquids proceeded with an efficiency comparable to that in tert-butyl alcohol [8], dioxane [57], or toluene... 

Other microbial lipases have also been successfully used in anhydrous ionic liquids, e.g., from Alcaligenes sp. (AsL) [54, 58], CaLA, Rhizomucor miehei lipase (RmL), and Thermomyces lanuginosus lipase (TIL) [54]. The lipase from pig pancreas (porcine pancreas lipase, PPL), the only mammalian lipase that has been subjected to ionic liquids, catalyzed transesterificationin[BMIm][NTf2]butnotin[BMIm][PF6]... 

The cutinase from Fusarium solani pisii maintained its transesterification activity in [BMIm][BF4], [OMIm][PF6] and [BMIm][PF6] (in order of increasing activity) at aw=0.2 [59]. Candida rugosa lipase (CrL), which is generally much less tolerant of anhydrous media than other microbial lipases, has successfully been used in anhydrous as well as water-saturated ionic liquids [60, 61, 62, 63, 64, 65]. 

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