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Lipase immobilized on hydrophobic microporous polypropylene for the hydrolysis of palm kernel olein

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Abstract

Lipase (triacylglycerol ester hydrolase, EC 3.1.1.3) fromRhizopus arrhizus was immobilized in this work by adsorption on microporous polypropylene and employed for the lipolysis of palm kernel olein. The optimum operating temperature for the lipolysis reaction was determined. The reaction follows Michaelis-Menten kinetics with product competitive inhibition for substrate concentrations in the range of 0.175–0.877M. The apparentK m and Vmax were 0.42M and 691 U/mg protein, respectively. A dissociation constant of the enzymeproduct complex,K I = 29.73 mM, for the product inhibition was also determined. Additionally, the time-courses of the reaction for various substrate concentrations were obtained and correlated sufficiently with those predicted from the theoretical rate equation for a period of up to 2 h. Experimental results indicated that discrepancies between the observed results and the predicted ones increase with reaction time.

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Abbreviations

ES*:

complex of enzyme and substrate molecules

Et :

total mass of enzyme in the reactor (mg)

k cat :

rate constantin the Michaelis-Menten equation (mmo1/min mg protein)

K I :

dissociation constant for the complex EP* (M)

K m :

apparent Michaelis constant (M)

P:

oleic acid concentration (M)

P0 :

initial concentrationof oleic acid (mM)

S:

substrate concentration based on ester bond (M)

S0 :

initial value of S (M)

t:

reaction time (min)

VI :

initial velocityof reaction (μmol/min)

Vmax :

apparent maximal velocity (μmol/min)

X:

conversion of substrate.

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Authors and Affiliations

  1. Department of Chemical Engineering, National Taiwan Institute of Technology, 10672, Taipei, Taiwan

    Yi-Hsu Ju & Fang-Cheng Huang

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  1. Yi-Hsu Ju
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  2. Fang-Cheng Huang
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Ju, YH., Huang, FC. Lipase immobilized on hydrophobic microporous polypropylene for the hydrolysis of palm kernel olein. Appl Biochem Biotechnol 55, 17–26 (1995). https://doi.org/10.1007/BF02788745

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  • DOI: https://doi.org/10.1007/BF02788745

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