Improvement of heat stability of yeast lipase by chemical modification with a heterobifunctional photogenerated reagent

Masaya Kawase, Kenji Sonomoto, Atsuo Tanaka

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

In order to improve the heat stability of purified lipase OF 360 from Candida cylindracea, lysine residues of the lipase were modified with a heterobifunctional photogenerated reagent, N-hydroxysuccinimide ester of 4-azidobenzoic acid, and photolyzed subsequently in the presence of decanol, which was proved to be a suitable heat stabilizer. The modified lipase showed excellent heat stability, even in the absence of decanol in the reaction system, compared to the native lipase. The activities of the modified lipase were retained about 70% after heating at 50°C for 15 min, while the native lipase lost about 80% of the original activities. The stabilization thus observed might be mainly caused by in situ formation of a cross-link between decanol and the lipase, and partly attributed to intra-molecular cross-linking in the lipase.

Original languageEnglish
Pages (from-to)155-157
Number of pages3
JournalJournal of Fermentation and Bioengineering
Volume70
Issue number3
DOIs
Publication statusPublished - Jan 1 1990
Externally publishedYes

Fingerprint

Chemical modification
Lipases
Lipase
Yeast
Hot Temperature
Yeasts
Heat stabilizers
Candida
Heating
Lysine
Esters
Stabilization
Acids

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Applied Microbiology and Biotechnology

Cite this

Improvement of heat stability of yeast lipase by chemical modification with a heterobifunctional photogenerated reagent. / Kawase, Masaya; Sonomoto, Kenji; Tanaka, Atsuo.

In: Journal of Fermentation and Bioengineering, Vol. 70, No. 3, 01.01.1990, p. 155-157.

Research output: Contribution to journalArticle

@article{a00ef7953e434f2b8228d38e121d2055,
title = "Improvement of heat stability of yeast lipase by chemical modification with a heterobifunctional photogenerated reagent",
abstract = "In order to improve the heat stability of purified lipase OF 360 from Candida cylindracea, lysine residues of the lipase were modified with a heterobifunctional photogenerated reagent, N-hydroxysuccinimide ester of 4-azidobenzoic acid, and photolyzed subsequently in the presence of decanol, which was proved to be a suitable heat stabilizer. The modified lipase showed excellent heat stability, even in the absence of decanol in the reaction system, compared to the native lipase. The activities of the modified lipase were retained about 70{\%} after heating at 50°C for 15 min, while the native lipase lost about 80{\%} of the original activities. The stabilization thus observed might be mainly caused by in situ formation of a cross-link between decanol and the lipase, and partly attributed to intra-molecular cross-linking in the lipase.",
author = "Masaya Kawase and Kenji Sonomoto and Atsuo Tanaka",
year = "1990",
month = "1",
day = "1",
doi = "10.1016/0922-338X(90)90175-V",
language = "English",
volume = "70",
pages = "155--157",
journal = "Journal of Bioscience and Bioengineering",
issn = "1389-1723",
publisher = "The Society for Biotechnology, Japan",
number = "3",

}

TY - JOUR

T1 - Improvement of heat stability of yeast lipase by chemical modification with a heterobifunctional photogenerated reagent

AU - Kawase, Masaya

AU - Sonomoto, Kenji

AU - Tanaka, Atsuo

PY - 1990/1/1

Y1 - 1990/1/1

N2 - In order to improve the heat stability of purified lipase OF 360 from Candida cylindracea, lysine residues of the lipase were modified with a heterobifunctional photogenerated reagent, N-hydroxysuccinimide ester of 4-azidobenzoic acid, and photolyzed subsequently in the presence of decanol, which was proved to be a suitable heat stabilizer. The modified lipase showed excellent heat stability, even in the absence of decanol in the reaction system, compared to the native lipase. The activities of the modified lipase were retained about 70% after heating at 50°C for 15 min, while the native lipase lost about 80% of the original activities. The stabilization thus observed might be mainly caused by in situ formation of a cross-link between decanol and the lipase, and partly attributed to intra-molecular cross-linking in the lipase.

AB - In order to improve the heat stability of purified lipase OF 360 from Candida cylindracea, lysine residues of the lipase were modified with a heterobifunctional photogenerated reagent, N-hydroxysuccinimide ester of 4-azidobenzoic acid, and photolyzed subsequently in the presence of decanol, which was proved to be a suitable heat stabilizer. The modified lipase showed excellent heat stability, even in the absence of decanol in the reaction system, compared to the native lipase. The activities of the modified lipase were retained about 70% after heating at 50°C for 15 min, while the native lipase lost about 80% of the original activities. The stabilization thus observed might be mainly caused by in situ formation of a cross-link between decanol and the lipase, and partly attributed to intra-molecular cross-linking in the lipase.

UR - http://www.scopus.com/inward/record.url?scp=0025096028&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025096028&partnerID=8YFLogxK

U2 - 10.1016/0922-338X(90)90175-V

DO - 10.1016/0922-338X(90)90175-V

M3 - Article

AN - SCOPUS:0025096028

VL - 70

SP - 155

EP - 157

JO - Journal of Bioscience and Bioengineering

JF - Journal of Bioscience and Bioengineering

SN - 1389-1723

IS - 3

ER -