Purification and characterization of a cold-active lipase from Pichia lynferdii Y-7723: pH-dependant activity deviation

Jae Han Bae, Mi Hyun Kwon, In-Hwan Kim, Ching T. Hou, Hak Ryul Kim

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Lipases with abnormal functionalities such as high thermostability and optimal activity at extreme conditions gain special attentions because of their applicability in the restricted reaction conditions. In particular, coldactive lipases have gained special attentions in various industrial fields such as washer detergent, pharmaceutical catalyst, and production of structured lipid. However, production of cold-active lipase is mostly found from psychrophilic microorganisms. Recently we found a novel cold-active lipase from Pichia lynferdii Y-7723 which is mesophilic yeast strain. In this study, we purified the cold active lipase and the enzyme was further characterized in several parameters. The enzyme was purified with 33 purification fold using chromatographic techniques and the purified lipase represented maximum lipolytic activity at 15°C and the maximum activity was highly dependent on pH.

Original languageEnglish
Pages (from-to)851-857
Number of pages7
JournalBiotechnology and Bioprocess Engineering
Volume19
Issue number5
DOIs
Publication statusPublished - 2014 Jan 1

Fingerprint

Pichia
Lipases
Lipase
Purification
Enzymes
Washers
Detergents
Microorganisms
Yeast
Drug products
Lipids
Yeasts
Catalysts
Pharmaceutical Preparations

Keywords

  • characterization
  • cold-active
  • lipase
  • pH-dependency
  • Pichia lynferdii

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology
  • Biomedical Engineering
  • Bioengineering

Cite this

Purification and characterization of a cold-active lipase from Pichia lynferdii Y-7723 : pH-dependant activity deviation. / Bae, Jae Han; Kwon, Mi Hyun; Kim, In-Hwan; Hou, Ching T.; Kim, Hak Ryul.

In: Biotechnology and Bioprocess Engineering, Vol. 19, No. 5, 01.01.2014, p. 851-857.

Research output: Contribution to journalArticle

@article{9f83dd4a510142c7904215dce9962933,
title = "Purification and characterization of a cold-active lipase from Pichia lynferdii Y-7723: pH-dependant activity deviation",
abstract = "Lipases with abnormal functionalities such as high thermostability and optimal activity at extreme conditions gain special attentions because of their applicability in the restricted reaction conditions. In particular, coldactive lipases have gained special attentions in various industrial fields such as washer detergent, pharmaceutical catalyst, and production of structured lipid. However, production of cold-active lipase is mostly found from psychrophilic microorganisms. Recently we found a novel cold-active lipase from Pichia lynferdii Y-7723 which is mesophilic yeast strain. In this study, we purified the cold active lipase and the enzyme was further characterized in several parameters. The enzyme was purified with 33 purification fold using chromatographic techniques and the purified lipase represented maximum lipolytic activity at 15°C and the maximum activity was highly dependent on pH.",
keywords = "characterization, cold-active, lipase, pH-dependency, Pichia lynferdii",
author = "Bae, {Jae Han} and Kwon, {Mi Hyun} and In-Hwan Kim and Hou, {Ching T.} and Kim, {Hak Ryul}",
year = "2014",
month = "1",
day = "1",
doi = "10.1007/s12257-014-0300-5",
language = "English",
volume = "19",
pages = "851--857",
journal = "Biotechnology and Bioprocess Engineering",
issn = "1226-8372",
publisher = "Korean Society for Biotechnology and Bioengineering",
number = "5",

}

TY - JOUR

T1 - Purification and characterization of a cold-active lipase from Pichia lynferdii Y-7723

T2 - pH-dependant activity deviation

AU - Bae, Jae Han

AU - Kwon, Mi Hyun

AU - Kim, In-Hwan

AU - Hou, Ching T.

AU - Kim, Hak Ryul

PY - 2014/1/1

Y1 - 2014/1/1

N2 - Lipases with abnormal functionalities such as high thermostability and optimal activity at extreme conditions gain special attentions because of their applicability in the restricted reaction conditions. In particular, coldactive lipases have gained special attentions in various industrial fields such as washer detergent, pharmaceutical catalyst, and production of structured lipid. However, production of cold-active lipase is mostly found from psychrophilic microorganisms. Recently we found a novel cold-active lipase from Pichia lynferdii Y-7723 which is mesophilic yeast strain. In this study, we purified the cold active lipase and the enzyme was further characterized in several parameters. The enzyme was purified with 33 purification fold using chromatographic techniques and the purified lipase represented maximum lipolytic activity at 15°C and the maximum activity was highly dependent on pH.

AB - Lipases with abnormal functionalities such as high thermostability and optimal activity at extreme conditions gain special attentions because of their applicability in the restricted reaction conditions. In particular, coldactive lipases have gained special attentions in various industrial fields such as washer detergent, pharmaceutical catalyst, and production of structured lipid. However, production of cold-active lipase is mostly found from psychrophilic microorganisms. Recently we found a novel cold-active lipase from Pichia lynferdii Y-7723 which is mesophilic yeast strain. In this study, we purified the cold active lipase and the enzyme was further characterized in several parameters. The enzyme was purified with 33 purification fold using chromatographic techniques and the purified lipase represented maximum lipolytic activity at 15°C and the maximum activity was highly dependent on pH.

KW - characterization

KW - cold-active

KW - lipase

KW - pH-dependency

KW - Pichia lynferdii

UR - http://www.scopus.com/inward/record.url?scp=84911375094&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84911375094&partnerID=8YFLogxK

U2 - 10.1007/s12257-014-0300-5

DO - 10.1007/s12257-014-0300-5

M3 - Article

AN - SCOPUS:84911375094

VL - 19

SP - 851

EP - 857

JO - Biotechnology and Bioprocess Engineering

JF - Biotechnology and Bioprocess Engineering

SN - 1226-8372

IS - 5

ER -