Geotrichum lipase

Enzymes PPL, lipase from Pseudomonas fluorescens F-AP, lipase from Rhizopus orizae AP-6, lipase from Aspergillus niger, SP-254, lipase from Aspergillus oryzae P-2, Chirazyme WCPC, whole cell cultures of Penicillium citrinum WCPFL, whole cell cultures of Pseudomona fluorescens CAL-B, lipase from Candida antarctica B PS-C, lipase from Pseudomonas cepacia GCL, lipase from Geotrichum candidum. n.r. not reported. 

Lipase (Geotrichum candidum) Ser217 Glu354 His463 [35]... 

Both of the aforementioned lipases contain Asp-His-Ser triades different catalytic triades can be found, e.g., in Geotrichum candidum (Glu-His-Ser) [7] or in Humkola lanuginosa (Asp-His-Tyr) [8]. 

Some hydrolases, especially the lipases from Candida rugosa (CRL) and Geotrichum candidum are sensitive to the acetaldehyde produced from reactions with... 

In a very similar way, acyl-enzyme formation depends upon the unsaturation level of the chains, and upon the position of the double bond(s) on the chains. Geotrichum candidum lipase is known to prefer fatty acids with a double bond on the C9. like oleic acid. 

Lipases can be classified into groups that reflect their specificity. The common lipases include non-specific lipases that do not discriminate between the position or the type of the fatty acid on the triacylglycerol (e.g., lipase from Candida cylindracea) and 1,3-specific lipases that act only at the sn-l and sn-3 positions of the triacylglycerol (e.g., lipases from Aspergillus niger and Rhizopus species). In addition, some lipases are specific for a specific fatty acid type (e.g., lipase from Geotrichum candidum). 

Fukumoto et al., 1963), A. oryzae (Arbigeetal., 1986), Geotrichum candidum (Jensen, 1974 Baillargeon and McCarthy, 1991), Candida cylindracea (Benzonana and Esposito, 1971), C. lipolytica (Alifax, 1979), Rhizopus dele-mar (Fukumoto et al., 1964), and Rh. arrhizus (Verhaeghe et al., 1990). The diversity of properties of these lipases, such as pH optimum and, in particular, specificity, enables the selection of an appropriate enzyme for a specific purpose (Kilara, 1985 Fox and Grufferty, 1991). 

Baillargeon, M.W., McCarthy, S.G. 1991. Geotrichum candidum NRRL Y-553 lipase purification, characterization and fatty acid specificity. Lipids 26, 831-836. 

Jensen, R.G. 1974. Characteristics of the lipase from the mold, Geotrichum candidum a review. Lipids 9, 149-157. 

The only known lipase that is nonspecific is the enzyme of a mold. Geotrichum candidum. It has a decided preference for fatty acids with a cis-A9 double bond such as oleic acid 14). There is no explanation for this specificity. The lipases of most other microorganisms are very similar to pancreatic lipase. For example, the lipase of the mold Rhizopus arrhizus is an exoenzyme which contains carbohydrates that are not essential for activity. It is not inhibited by DFP, it is specific for primary ester groups, and it does not distinguish between diflEerent fatty acids (15). Other microbial lipases are similar in these respects but may diflFer in their recognition of steric hindrance. The lipase of Stapyhlococcus aureus... 

Clearly, high-resolution three-dimensional structures were needed to address these problems. The first crystallographic study of a lipase is credited to Hata et al. (1979), who investigated the structure of a fungal enzyme (GcL) from Geotrichum candidum, although at a very low resolu-... 

Abbreviations GcL, Geotrichum candidum lipase hPL, human pancreatic lipase RmL, Rhizomucor miehei lipase hHL, human hepatic lipase hLPL, human lipoprotein lipase hLAL, human lysosomal acid lipase hGL, human gastric lipase BAL, bile salt-activated lipase HSL, hormone-sensitive lipase CLP, colipase AChE, Torpedo cal omica acetylcholinesterase cDNA, complementary deoxyribonucleic acid VLDL, very low-density lipoprotein IDL, intermediate-density lipoprotein HDL, high-density lipoprotein apoC-II, apolipoprotein C-II. 

M. (1991) Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum. Nature 351, 761—764... 

Table 11.1-18. Lipase-catalyzed enantiotopos-differentiating acylation of prochiral cyclic diols in organic solvents (PPL pig pancreas lipase, PFL Pseudomonasfluorescens lipase, PCL Pseudomonas cepacia lipase, CCL Candida cylindracea lipase, MSL Mucor sp. lipase, CVL Chromobacterium viscosum lipase, GCL Geotrichum candidum lipase, CRL Candida rugosa lipase, MML Mucor miehei lipase, CAL-B Candida antarctica B lipase, LIP Pseudomonas sp. lipase-Toyobo).

Other methods used to quantify free fat include centrifugation in Babcock or Gerber butyrometers at 40-60°C (the free fat is read off directly on the graduated scale) release of membrane-bound enzymes, especially xanthine oxidase or alkaline phosphatase, or the susceptibility of milk fat to hydrolysis by added lipase (e.g. from Geotrichum candidum). 

Lipases specific for a particular class of fatty acids Geotrichum candidum has been found specific for omega-9 fatty acids others are specific for short-chain fatty acids, and still others for long-chain fatty acids... 

Lipolysis in mould-ripened varieties is due primarily to the lipases of Penicillium roqueforti or P. camemberti, which secrete potent extracellular lipases. Penicillium lipases are well characterized (see Kinsella and Hwang, 1976 Gripon, 1987,1993). P. camemberti appears to excrete only one lipase which is optimally active at ca. pH 9.0 and at ca. 35°C. P. roqueforti excretes two lipases, one with a pH optimum at 7.5 to 8.0 (or perhaps 9.0 to 9.5), the other at pH 6.0 to 6.5 The acid and alkaline lipases exhibit different specificities. Lipases of Geotrichum candidum have been studied by Side-bottom et al. (1991) and Charlton et al. (1992). This organism produces two lipases of different substrate specificities. 

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