On the interfacial activation of Candida antarctica lipase A and B as compared with Humicola lanuginosa lipase

Martinelle, Mats; Holmquist, Mats; Hult, Karl

doi:10.1016/0005-2760(95)00131-u

Cited by 330 publications

(294 citation statements)

References 23 publications

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“…Of these forms, lipase B is stereoselective towards the R-isomer of ketoprofen in an achiral solvent such as isopentyl methyl ketone and also in S(+)-carvone (Arroyo and Sinisterra, 1995). Martinelle et al (1995) studied interfacial activation of C. antarctica lipases A and B (CALB) and compared them with the Humicola lanuginosa lipase. CALB displayed no interfacial activation, which indicated an absence of the lid structure that regulates the access to the active site.…”

Section: Multiple Forms Of Lipasesmentioning

confidence: 99%

“…Lipases catalyze the hydrolysis of triacylglycerols to glycerol and free fatty acids. In contrast to esterases, lipases are activated only when adsorbed to an oil-water interface (Martinelle et al, 1995) and do not hydrolyze dissolved substrates in the bulk fluid. A true lipase will split emulsified esters of glycerine and long-chain fatty acids such as triolein and tripalmitin.…”

Section: Introductionmentioning

confidence: 99%

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Production, purification, characterization, and applications of lipases

Sharma

Chisti

Banerjee

2001

Biotechnology Advances

1,284

712

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Lipases (triacylglycerol acylhydrolases, EC 3.1.1.3) catalyze the hydrolysis and the synthesis of esters formed from glycerol and long-chain fatty acids. Lipases occur widely in nature, but only microbial lipases are commercially significant. The many applications of lipases include speciality organic syntheses, hydrolysis of fats and oils, modification of fats, flavor enhancement in food processing, resolution of racemic mixtures, and chemical analyses. This article discusses the production, recovery, and use of microbial lipases. Issues of enzyme kinetics, thermostability, and bioactivity are addressed. Production of recombinant lipases is detailed. Immobilized preparations of lipases are discussed. In view of the increasing understanding of lipases and their many applications in high-value syntheses and as bulk enzymes, these enzymes are having an increasing impact on bioprocessing. D

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Section: Multiple Forms Of Lipasesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Production, purification, characterization, and applications of lipases

Sharma

Chisti

Banerjee

2001

Biotechnology Advances

1,284

712

View full text Add to dashboard Cite

show abstract

“…With respect to lipase activity, ROL w displays a 3.7 fold increase in k cat /K Mapp values compared to ROL29, when using TC 4 …”

Section: Chain Length Selectivity and Kinetic Parameters Of Rol W Lipasementioning

confidence: 95%

“…Lipases are ubiquitous enzymes of considerable physiological significance and industrial potential and catalyze the hydrolysis of triacylglycerols to glycerol and free fatty acids. In contrast to esterases, lipases are activated only when adsorbed to an oil-water interface [3][4][5] and do not hydrolyse dissolved substrates in the bulk fluid. A true lipase will split emulsified esters of glycerin long-chain fatty acids such as triolein and tripalmitin.…”

Section: Introductionmentioning

confidence: 99%

Comparative study of kinetic and interfacial properties of a novelRhizopus oryzaelipase and ROL29

Salah¹,

Mosbah²,

Gargouri³

et al. 2007

OCL

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“…[25,26]. Martinelle and co. workers [27] observed the level of enzymatic activity change of LIP CA , in the presence of SDS, was found to be insignificant but in contrast, measured an increase in enzymatic activity for LIP HLL in the presence of SDS. This is supportive of the findings we observed of SDS in our study and although we measured LIP HLL exhibiting a trend towards greater activity in the presence of SDS (Figure 6), this was not determined to be significant.…”

Section: Enzymatic Assay Of Catalytic Latex Filmsmentioning

confidence: 96%