Lipolytic Activity of Microorganisms at Low and Intermediate Temperatures. III. Activity of Microbial Lipases at Temperatures Below 0°C

Alford, John A.; Pierce, David A.

doi:10.1111/j.1365-2621.1961.tb00399.x

Cited by 89 publications

(32 citation statements)

References 5 publications

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“…C. antarctica isolated from Antarctic habitat is a wellknown source for two industrially important CLPs, CAL-A and CAL-B (de Maria et al 2005). Other fungi and yeast reported to produce cold active lipase include Candida lipolytica, Geotrichum candidum and Pencillium roqueforti isolated from frozen food samples (Alford & Pierce 1961).…”

Section: Sources Of Clpsmentioning

confidence: 99%

Cold active lipases – an update

Kavitha

2016

Frontiers in Life Science

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Cold active lipases (CLPs) are gaining importance nowadays as they are increasingly used in fine chemical synthesis, bioremediation, food processing and as detergent additive. These enzymes exhibit high catalytic activity at low temperatures and flexibility to act at low water medium. Since they are active at low temperatures consume less energy and also stabilize fragile compounds in the reaction medium. CLPs are commonly obtained from psychrophilic microorganisms which thrive in cold habitats. Compared to mesophilic and thermophilic lipases, only a few CLPs were studied and industrially exploited so far. CLPs (C. antarctica lipase-A and C. antarctica lipase-B) from Candida antarctica isolated from Antarctic region are the well studied and industrially employed, and many are being followed up. This review updates the CLPs reported recently and the industrial applications of CLPs. ARTICLE HISTORY

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Section: Sources Of Clpsmentioning

confidence: 99%

Cold active lipases – an update

Kavitha

2016

Frontiers in Life Science

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“…Lipases I and I1 are 84% identical at the amino acid level and these enzymes show some similarity (45%) with an extracellular lipase from Candidu rugosa [22 -341. There is no amino acid sequence similarity between this lipase and other lipases apart from a possible active site motif: Gly-Xaa-Ser-Xaa-GlyIn view of the unique specificity for unsaturated substrates reported for a lipase secreted by G. candidum [5], we have endeavoured to purify extracellular lipases synthesized by ATCC 34614 and CMICC 335426 strains and to characterize (22 -241. …”

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confidence: 99%

“…The most extreme example of this is an extracellular lipase isolated by Alford and Pierce from a strain of the mould Geotrichum candidum which has been reported to have a specificity for unsaturated substrates [5]. This enzyme has not been purified and the original strain was thought to be no longer in existence [6].…”

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Geotrichum candidum produces several lipases with markedly different substrate specificities

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Charton

Dunn

et al. 1991

European Journal of Biochemistry

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We have purified and examined the substrate specificity of four lipases from two strains of the mould Geotrichum candidum, ATCC 34614 and CMICC 335426. We have designated the lipases I and I1 (ATCC 34614), and A and B (CMICC 335426). The enzymes are monomeric and have similar molecular masses and pl. Thus, lipases I and I1 have native molecular masses of 50.1 kDa and 55.5 kDa, and p l o f 4.61 and 4.47, respectively.Lipases A and B are very similar to lipases I and I1 with native molecular masses of 53.7 kDa and 48.9 kDa, and p l of 4.71 and 4.50, respectively. Treatment with endo-P-N-acetylglucosaminidase caused a reduction in molecular mass of approximately 4.5 kDa for all four lipases, indicating that these enzymes are glycosylated. Western blotting shows that the lipases are related. However, lipase B from CMICC 335426 shows a remarkable specificity for unsaturated substrates with a double bond at position 9 (cis configuration), and this specificity is not exhibited by the other three lipases. No lipase of this unique specificity has previously been purified to homogeneity. Structural studies using these four lipases should allow insight into the molecular basis of this remarkable specificity.Lipases (glycerol ester hydrolases) catalyse the hydrolysis of ester linkages in lipids with the release of the constituent alcohol and acid moieties. They act at the interface between a substrate phase, which has a very low solubility in water, and an aqueous phase in which the enzyme is dissolved [l]. These enzymes can differ considerably in their positional specificity for the hydrolysis of fatty acid from a triacylglycerol backbone [2, 31. Advantage is taken of this, industrially, in the production of cocoa butter equivalents from cheap starting materials [4].In addition to positional specificity, lipases have been reported to have specificity for the fatty acids which are hydrolyzed. The most extreme example of this is an extracellular lipase isolated by Alford and Pierce from a strain of the mould Geotrichum candidum which has been reported to have a specificity for unsaturated substrates [5]. This enzyme has not been purified and the original strain was thought to be no longer in existence [6]. However, in 1969 our laboratory received a strain of G. candidum from Dr Alford, and this has now been deposited at the Commonwealth Mycological Institute Collection as CMICC 335426.Tsujisaka et al. have purified a lipase from G. candidum ATCC 34614 to homogeneity [7], and this does not appear to show the same substrate specificity as the enzyme isolated by Alford and Pierce [8,9] [19], and these lipases could possess different substrate specificities. Specificity studies of crude extracts can therefore be complicated by the presence of more than one lipase. Sugihara et al. [16] have, however, reported the purification of two lipases from G. candidurn ATCC 34614, but the two enzymes appear to display the same substrate specificity towards a variety of triglycerides.To appreciate the relationship between substrate specific...

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“…It is difficult to identify the reasons for changes in fats, for example, to separate chemical from microbial oxidation. In addition, some of the products formed during either protein or fat degradation (e.g., carboxyl-containing compounds) may be further metabolized by certain species of microbes (Alford and Pierce, 1961). The significance of various biochemical changes have been reviewed (Ingram and Dainty, 1971).…”

Section: Spoilage Of Chilled Meatmentioning

confidence: 99%

Rapid method for detection of muramic acid and cadaverine as indicators of microbial load on fresh meats

Lebron

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Lipolytic Activity of Microorganisms at Low and Intermediate Temperatures. III. Activity of Microbial Lipases at Temperatures Below 0°C

Cited by 89 publications

References 5 publications

Cold active lipases – an update

Cold active lipases – an update

Geotrichum candidum produces several lipases with markedly different substrate specificities

Rapid method for detection of muramic acid and cadaverine as indicators of microbial load on fresh meats

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