2017
DOI: 10.4014/jmb.1608.08005
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Purification and Properties of Extracellular Lipases with Transesterification Activity and 1,3-Regioselectivity from Rhizomucor miehei and Rhizopus oryzae

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Cited by 36 publications
(37 citation statements)
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References 31 publications
(44 reference statements)
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“…There was observable and slight increase in pNPP hydrolysis by the lipase from R. miehei. Overall, the two enzymes were more stable in methanol and ethanol at higher concentrations than other alcohols tested [68]. Addition of 70% methanol showed maximum lipolytic activity while 2-propanol showed the minimum activity by lipase from Microbacterium sp isolated from marble mining rock, New Delhi [5].…”
Section: Effect Of Solventsmentioning
confidence: 84%
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“…There was observable and slight increase in pNPP hydrolysis by the lipase from R. miehei. Overall, the two enzymes were more stable in methanol and ethanol at higher concentrations than other alcohols tested [68]. Addition of 70% methanol showed maximum lipolytic activity while 2-propanol showed the minimum activity by lipase from Microbacterium sp isolated from marble mining rock, New Delhi [5].…”
Section: Effect Of Solventsmentioning
confidence: 84%
“…In addition to esterification of long chain fatty acids and glycerol into triacylglycerides, as well as acting on other reactions such as transesterification and alcoholysis makes lipases a great biocatalyst of interest in organic chemistry and evaluating their stability in organic media is essential for further reaction design such as in biodiesel production [14,68]. Lipase immobilized on octyl derivative was very stable in glycerol.…”
Section: Effect Of Solventsmentioning
confidence: 99%
“…Lipase produced from Yarrowia lipolytica showed maximum activity toward p-nitrophenyl caprylate [31]. Purified enzymes from R. oryzae and Rhizopus miehei had almost equal affinity to the substrate p-nitrophenyl palmitate, but the R. oryzae lipasecatalyzed p-nitrophenyl palmitate hydrolysis was about 1.13 times faster than that determined for the R. miehei enzyme [18]. In another study, lipase showed highest activity when pnitrophenyl butyrate (p-NPB) was used at a concentration of 30 mM [32].…”
Section: Discussionmentioning
confidence: 99%
“…1. The purified fractions 16,17,18,19,20,21,22,23,24,25, and 26 showed maximum specific activity and were pooled together (Fig. 1).…”
Section: Purificationmentioning
confidence: 99%
“…properties of most lipases are the ability to catalyze enzymatic interesterification reactions rearranging a triglyceride molecule, as well as those of transesterification between oily compounds, alkyl or aryl esters, and alcohols. Lipases can also be used to accelerate the degradation of fatty residues and polyurethane (TAKÓ et al, 2017).…”
Section: Introductionmentioning
confidence: 99%