Modification of phospholipids with lipases and phospholipases

Annikka Mustranta, Pirkko Forssell, Anna-Marja Aura, Tapani Suortti, Kaisa Poutanen

Research output: Contribution to journalArticleScientificpeer-review

20 Citations (Scopus)

Abstract

Different commercial lipases and phosphoiipases were studied in the hydrolysis and transesterification of synthetic phosphatidylcholine and soybean lecithin. Wide variations in the lipase and phospholipase activities and in the protein contents of the preparations were observed. The substrate specificity varied between different enzymes. A high degree of hydrolysis of synthetic and soybean phospholipids was achieved with both types of enzymes.
Enzymes immobilized on Celite were used in the transesterification of dimyristoyl phosphatidylcholine and oleic acid. The conversions were carried out both without solvent and in the presence of toluene. The amount of modified phosphatidylcholine was measured using HPLC. The highest amount of modified phosphatidylcholine was obtained in solvent-free transesterification. The best results were obtained with Aspergillus niyer lipase.
Original languageEnglish
Pages (from-to)181 - 194
JournalBiocatalysis and Biotransformation
Volume9
Issue number1-4
DOIs
Publication statusPublished - 1994
MoE publication typeA1 Journal article-refereed

Fingerprint

Phospholipases
Transesterification
Phospholipids
Lipases
Lipase
Phosphatidylcholines
Enzymes
Hydrolysis
Soybeans
Lecithin
Oleic acid
Aspergillus
Diatomaceous Earth
Immobilized Enzymes
Toluene
Lecithins
Oleic Acid
Substrate Specificity
Proteins
High Pressure Liquid Chromatography

Keywords

  • modification
  • phospholipids
  • phospholilipases
  • lipases

Cite this

Mustranta, Annikka ; Forssell, Pirkko ; Aura, Anna-Marja ; Suortti, Tapani ; Poutanen, Kaisa. / Modification of phospholipids with lipases and phospholipases. In: Biocatalysis and Biotransformation. 1994 ; Vol. 9, No. 1-4. pp. 181 - 194.
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Modification of phospholipids with lipases and phospholipases. / Mustranta, Annikka; Forssell, Pirkko; Aura, Anna-Marja; Suortti, Tapani; Poutanen, Kaisa.

In: Biocatalysis and Biotransformation, Vol. 9, No. 1-4, 1994, p. 181 - 194.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Modification of phospholipids with lipases and phospholipases

AU - Mustranta, Annikka

AU - Forssell, Pirkko

AU - Aura, Anna-Marja

AU - Suortti, Tapani

AU - Poutanen, Kaisa

PY - 1994

Y1 - 1994

N2 - Different commercial lipases and phosphoiipases were studied in the hydrolysis and transesterification of synthetic phosphatidylcholine and soybean lecithin. Wide variations in the lipase and phospholipase activities and in the protein contents of the preparations were observed. The substrate specificity varied between different enzymes. A high degree of hydrolysis of synthetic and soybean phospholipids was achieved with both types of enzymes.Enzymes immobilized on Celite were used in the transesterification of dimyristoyl phosphatidylcholine and oleic acid. The conversions were carried out both without solvent and in the presence of toluene. The amount of modified phosphatidylcholine was measured using HPLC. The highest amount of modified phosphatidylcholine was obtained in solvent-free transesterification. The best results were obtained with Aspergillus niyer lipase.

AB - Different commercial lipases and phosphoiipases were studied in the hydrolysis and transesterification of synthetic phosphatidylcholine and soybean lecithin. Wide variations in the lipase and phospholipase activities and in the protein contents of the preparations were observed. The substrate specificity varied between different enzymes. A high degree of hydrolysis of synthetic and soybean phospholipids was achieved with both types of enzymes.Enzymes immobilized on Celite were used in the transesterification of dimyristoyl phosphatidylcholine and oleic acid. The conversions were carried out both without solvent and in the presence of toluene. The amount of modified phosphatidylcholine was measured using HPLC. The highest amount of modified phosphatidylcholine was obtained in solvent-free transesterification. The best results were obtained with Aspergillus niyer lipase.

KW - modification

KW - phospholipids

KW - phospholilipases

KW - lipases

U2 - 10.3109/10242429408992119

DO - 10.3109/10242429408992119

M3 - Article

VL - 9

SP - 181

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JO - Biocatalysis and Biotransformation

JF - Biocatalysis and Biotransformation

SN - 1024-2422

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