A study on the lipid-coating of lipases

Yoshiaki Sugimura, Kimitoshi Fukunaga, Takahiro Matsuno, Katsumi Nakao, Masahiro Goto, Fumiyuki Nakashio

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

A quantitative study on the lipid-coating of lipases together with soluble globular proteins such as bovin serum albumin and γ-globulin was carried out using a synthetic lipid, dioleyl glucosyl L-glutamate, by means of a solution depletion method. Complexation isotherms similar to Langmuir-type adsorption isotherms with saturation plateaus were derived from the results, and additional parameters, such as the number of complexation sites (n) and the complexation constant (K), were also evaluated. Together, these data provide a more detailed description of the lipid-coating process. For example, it is possible to predict the coverage of proteins, the number of lipid molecules bound per protein molecule, the maximum values of this number, and the compositions of the precipitated lipid-coated protein under the given lipid-coating conditions. The positive correlation among protein surface hydrophobicity, coverage of protein, and diminished amounts of the lipid molecules required to hydrophobize an original protein confirms that the affinity between protein and lipid in this process is primarily hydrophobic, and that the lipid-coating of enzymes seems to be limited by intrinsic structural features of the enzymes themselves. The reactivity of the lipid-coated lipase in organic solvents depends on the pH of the aqueous solution in the complexation and shows the same profile as that of native lipase in aqueous solution, while the coverage of lipases is scarcely influenced by aqueous pH. The coverage of lipase had no influence on specific activity or enantioselectivity in the enzymatic reaction in organic solvent.

Original languageEnglish
Pages (from-to)137-143
Number of pages7
JournalBiochemical Engineering Journal
Volume2
Issue number2
DOIs
Publication statusPublished - Nov 1 1998

Fingerprint

Lipases
Lipase
Lipids
Coatings
Proteins
Complexation
Organic solvents
Molecules
Enzymes
Serum Globulins
Enantioselectivity
Globulins
Hydrophobicity
Hydrophobic and Hydrophilic Interactions
Adsorption isotherms
Serum Albumin
Adsorption
Isotherms
Glutamic Acid
Membrane Proteins

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Environmental Engineering
  • Biomedical Engineering

Cite this

Sugimura, Y., Fukunaga, K., Matsuno, T., Nakao, K., Goto, M., & Nakashio, F. (1998). A study on the lipid-coating of lipases. Biochemical Engineering Journal, 2(2), 137-143. https://doi.org/10.1016/S1369-703X(98)00026-6

A study on the lipid-coating of lipases. / Sugimura, Yoshiaki; Fukunaga, Kimitoshi; Matsuno, Takahiro; Nakao, Katsumi; Goto, Masahiro; Nakashio, Fumiyuki.

In: Biochemical Engineering Journal, Vol. 2, No. 2, 01.11.1998, p. 137-143.

Research output: Contribution to journalArticle

Sugimura, Y, Fukunaga, K, Matsuno, T, Nakao, K, Goto, M & Nakashio, F 1998, 'A study on the lipid-coating of lipases', Biochemical Engineering Journal, vol. 2, no. 2, pp. 137-143. https://doi.org/10.1016/S1369-703X(98)00026-6
Sugimura Y, Fukunaga K, Matsuno T, Nakao K, Goto M, Nakashio F. A study on the lipid-coating of lipases. Biochemical Engineering Journal. 1998 Nov 1;2(2):137-143. https://doi.org/10.1016/S1369-703X(98)00026-6
Sugimura, Yoshiaki ; Fukunaga, Kimitoshi ; Matsuno, Takahiro ; Nakao, Katsumi ; Goto, Masahiro ; Nakashio, Fumiyuki. / A study on the lipid-coating of lipases. In: Biochemical Engineering Journal. 1998 ; Vol. 2, No. 2. pp. 137-143.
@article{ba69b77e36c249398e180928a0fd0f1b,
title = "A study on the lipid-coating of lipases",
abstract = "A quantitative study on the lipid-coating of lipases together with soluble globular proteins such as bovin serum albumin and γ-globulin was carried out using a synthetic lipid, dioleyl glucosyl L-glutamate, by means of a solution depletion method. Complexation isotherms similar to Langmuir-type adsorption isotherms with saturation plateaus were derived from the results, and additional parameters, such as the number of complexation sites (n) and the complexation constant (K), were also evaluated. Together, these data provide a more detailed description of the lipid-coating process. For example, it is possible to predict the coverage of proteins, the number of lipid molecules bound per protein molecule, the maximum values of this number, and the compositions of the precipitated lipid-coated protein under the given lipid-coating conditions. The positive correlation among protein surface hydrophobicity, coverage of protein, and diminished amounts of the lipid molecules required to hydrophobize an original protein confirms that the affinity between protein and lipid in this process is primarily hydrophobic, and that the lipid-coating of enzymes seems to be limited by intrinsic structural features of the enzymes themselves. The reactivity of the lipid-coated lipase in organic solvents depends on the pH of the aqueous solution in the complexation and shows the same profile as that of native lipase in aqueous solution, while the coverage of lipases is scarcely influenced by aqueous pH. The coverage of lipase had no influence on specific activity or enantioselectivity in the enzymatic reaction in organic solvent.",
author = "Yoshiaki Sugimura and Kimitoshi Fukunaga and Takahiro Matsuno and Katsumi Nakao and Masahiro Goto and Fumiyuki Nakashio",
year = "1998",
month = "11",
day = "1",
doi = "10.1016/S1369-703X(98)00026-6",
language = "English",
volume = "2",
pages = "137--143",
journal = "Biochemical Engineering Journal",
issn = "1369-703X",
publisher = "Elsevier",
number = "2",

}

TY - JOUR

T1 - A study on the lipid-coating of lipases

AU - Sugimura, Yoshiaki

AU - Fukunaga, Kimitoshi

AU - Matsuno, Takahiro

AU - Nakao, Katsumi

AU - Goto, Masahiro

AU - Nakashio, Fumiyuki

PY - 1998/11/1

Y1 - 1998/11/1

N2 - A quantitative study on the lipid-coating of lipases together with soluble globular proteins such as bovin serum albumin and γ-globulin was carried out using a synthetic lipid, dioleyl glucosyl L-glutamate, by means of a solution depletion method. Complexation isotherms similar to Langmuir-type adsorption isotherms with saturation plateaus were derived from the results, and additional parameters, such as the number of complexation sites (n) and the complexation constant (K), were also evaluated. Together, these data provide a more detailed description of the lipid-coating process. For example, it is possible to predict the coverage of proteins, the number of lipid molecules bound per protein molecule, the maximum values of this number, and the compositions of the precipitated lipid-coated protein under the given lipid-coating conditions. The positive correlation among protein surface hydrophobicity, coverage of protein, and diminished amounts of the lipid molecules required to hydrophobize an original protein confirms that the affinity between protein and lipid in this process is primarily hydrophobic, and that the lipid-coating of enzymes seems to be limited by intrinsic structural features of the enzymes themselves. The reactivity of the lipid-coated lipase in organic solvents depends on the pH of the aqueous solution in the complexation and shows the same profile as that of native lipase in aqueous solution, while the coverage of lipases is scarcely influenced by aqueous pH. The coverage of lipase had no influence on specific activity or enantioselectivity in the enzymatic reaction in organic solvent.

AB - A quantitative study on the lipid-coating of lipases together with soluble globular proteins such as bovin serum albumin and γ-globulin was carried out using a synthetic lipid, dioleyl glucosyl L-glutamate, by means of a solution depletion method. Complexation isotherms similar to Langmuir-type adsorption isotherms with saturation plateaus were derived from the results, and additional parameters, such as the number of complexation sites (n) and the complexation constant (K), were also evaluated. Together, these data provide a more detailed description of the lipid-coating process. For example, it is possible to predict the coverage of proteins, the number of lipid molecules bound per protein molecule, the maximum values of this number, and the compositions of the precipitated lipid-coated protein under the given lipid-coating conditions. The positive correlation among protein surface hydrophobicity, coverage of protein, and diminished amounts of the lipid molecules required to hydrophobize an original protein confirms that the affinity between protein and lipid in this process is primarily hydrophobic, and that the lipid-coating of enzymes seems to be limited by intrinsic structural features of the enzymes themselves. The reactivity of the lipid-coated lipase in organic solvents depends on the pH of the aqueous solution in the complexation and shows the same profile as that of native lipase in aqueous solution, while the coverage of lipases is scarcely influenced by aqueous pH. The coverage of lipase had no influence on specific activity or enantioselectivity in the enzymatic reaction in organic solvent.

UR - http://www.scopus.com/inward/record.url?scp=0000255311&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0000255311&partnerID=8YFLogxK

U2 - 10.1016/S1369-703X(98)00026-6

DO - 10.1016/S1369-703X(98)00026-6

M3 - Article

AN - SCOPUS:0000255311

VL - 2

SP - 137

EP - 143

JO - Biochemical Engineering Journal

JF - Biochemical Engineering Journal

SN - 1369-703X

IS - 2

ER -