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Rigorous kinetic model considering positional specificity of lipase for enzymatic stepwise hydrolysis of triolein in biphasic oil–water system

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Abstract

A rigorous kinetic model describing the stepwise triglyceride hydrolysis at the oil–water interface, based on the Ping Pong Bi Bi mechanism using suspended lipase having positional specificity, was constructed. The preference of the enzyme to cleave to the ester bonds at the edge and the center of the glycerol backbone of the substrates (tri-, di- or monoglyceride) was incorporated in the model. This model was applied to the experimental results for triolein hydrolysis using suspended Porcine pancreatic lipase (an sn-1,3 specific lipase) and Candida rugosa lipase (a non-specific lipase) in a biphasic oil–water system under various operating conditions. In order to discuss the model’s advantages, other models that do not consider the positional specificity of the lipase were also applied to our experimental results. The model considering the positional specificity of the lipase gave results which fit better with the experimental data and described the effect of the initial enzyme concentration, the interfacial area, and the initial concentrations of triolein on the entire process of the stepwise triolein hydrolysis. This model also gives a good representation of the rate for cleaving the respective ester bonds of each substrate by each type of lipase.

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Abbreviations

A :

Oil–water interfacial area (m2)

C E :

Concentration of enzyme (kg m−3)

C E,0 :

Initial concentration of enzyme (kg m−3)

C i :

Concentrations of component i (mol m−3)

k1 to k14:

Rate constants of elementary reactions shown in Fig. 2

K E :

Adsorption constant of enzyme (m3 kg−1)

K i :

Adsorption constant of component i (m)

q Ei :

Concentrations of enzyme component i complexes adsorbed at interface (mol m−2)

q F :

Concentration of acylated form of enzyme complex adsorbed at interface (mol m−2)

q E,max :

Saturated concentration of enzyme adsorbed at interface (kg m−2)

q E,tot :

Total concentration of enzyme adsorbed at interface (kg m−2)

q i :

Concentrations of component i adsorbed at interface (mol m−2)

v i :

Reaction rates of component i adsorbed at interface (mol m−2 h−1)

V w :

Volume of water phase (m3)

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Authors and Affiliations

  1. Department of Chemical Engineering, Faculty of Engineering, University of Indonesia, Depok, 16424, Indonesia

    Heri Hermansyah & Anondho Wijanarko

  2. Department of Chemical Engineering, Tohoku University, Sendai, 980-8579, Japan

    Masaki Kubo, Naomi Shibasaki-Kitakawa & Toshikuni Yonemoto

Authors
  1. Heri Hermansyah
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  2. Anondho Wijanarko
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  3. Masaki Kubo
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  4. Naomi Shibasaki-Kitakawa
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  5. Toshikuni Yonemoto
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Correspondence to Heri Hermansyah.

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Hermansyah, H., Wijanarko, A., Kubo, M. et al. Rigorous kinetic model considering positional specificity of lipase for enzymatic stepwise hydrolysis of triolein in biphasic oil–water system. Bioprocess Biosyst Eng 33, 787–796 (2010). https://doi.org/10.1007/s00449-009-0400-3

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  • DOI: https://doi.org/10.1007/s00449-009-0400-3

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