Uniqueness of microbial cutinases in hydrolysis of p-nitrophenyl esters

Yang Hoon Kim, Jeewon Lee, Seung Hyeon Moon

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

Using fungal (Fusarium solani f. pisi) and bacterial (Pseudomonas mendocina) cutinases, the initial hydrolysis rate of p-nitrophenyl esters was systematically estimated for a wide range of enzyme and substrate concentrations using a 96-well microplate reader. Both cutinases exhibited a high substrate specificity; i.e. a high hydrolytic activity on p-nitrophenyl butyrate (PNB), yet extremely low activity on p-nitrophenyl palmitate (PNP). When compared to the hydrolysis of PNB and PNP by other hydrolases [lipases and esterases derived from different microbial sources, such as bacteria (Pseudomonas cepacia, Pseudomonas flurescens, Bacillus stearothermophilus), molds (Aspergillus niger, Mucor miehei), and yeasts (Candida rugosa, Candida cylindracea)], the above substrate specificity would seem to be a unique characteristic of cutinases. Secondly, the hydrolytic activity of the cutinases on PNB appeared much faster than that of the other hydrolytic enzymes mentioned above. Furthermore, the current study proved that even when the cutinases were mixed with large amounts of other hydrolases (lipases or esterases), the initial hydrolysis rate of PNB was determined only by the cutinase concentration for each PNB concentration. This property of cutinase activity would seem to result from a higher accessibility to the substrate PNB, compared with the other hydrolytic enzymes. Accordingly, these distinct properties of cutinases may be very useful in the rapid and easy isolation of various natural cutinases with different microbial sources, each of which may provide a novel industrial application with a specific enzymatic function.

Original languageEnglish
Pages (from-to)57-63
Number of pages7
JournalJournal of Microbiology and Biotechnology
Volume13
Issue number1
Publication statusPublished - 2003 Feb 1

Fingerprint

Hydrolysis
Esters
Hydrolases
Enzymes
Candida
Lipases
Substrates
Aspergillus
Molds
Bacilli
Palmitates
Yeast
Esterases
Substrate Specificity
Industrial applications
Lipase
Bacteria
Pseudomonas mendocina
Burkholderia cepacia
Mucor

Keywords

  • Accessibility
  • Cutinase
  • Esterase
  • Hydrolysis
  • Lipase
  • Substrate specificity

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology
  • Microbiology

Cite this

Uniqueness of microbial cutinases in hydrolysis of p-nitrophenyl esters. / Kim, Yang Hoon; Lee, Jeewon; Moon, Seung Hyeon.

In: Journal of Microbiology and Biotechnology, Vol. 13, No. 1, 01.02.2003, p. 57-63.

Research output: Contribution to journalArticle

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