Affinity purification and characterization of a biodegradable plastic-degrading enzyme from a yeast isolated from the larval midgut of a stag ... View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2013-09

AUTHORS

Ken Suzuki, Hironori Sakamoto, Yukiko Shinozaki, Jun Tabata, Takashi Watanabe, Atsushi Mochizuki, Motoo Koitabashi, Takeshi Fujii, Seiya Tsushima, Hiroko K. Kitamoto

ABSTRACT

Two yeast strains, which have the ability to degrade biodegradable plastic films, were isolated from the larval midgut of a stag beetle, Aegus laevicollis. Both of them are most closely related to Cryptococcus magnus and could degrade biodegradable plastic (BP) films made of poly(butylene succinate) (PBS) and poly(butylene succinate-co-adipate) (PBSA) effectively. A BP-degrading enzyme was purified from the culture broth of one of the isolated strains employing a newly developed affinity purification method based on the binding action of the enzyme to the substrate (emulsified PBSA) and its subsequent degradative action toward the substrate. Partial amino acid sequences of this enzyme suggested that it belongs to the cutinase family, and thus, the enzyme was named CmCut1. It has a molecular mass of 21 kDa and a degradative activity for emulsified PBSA which was significantly enhanced by the simultaneous presence of Ca(2+) or Mg(2+) at a concentration of about 2.5 mM. Its optimal pH was 7.5, and the optimal temperature was 40 °C. It showed a broad substrate specificity for p-nitrophenyl (pNP)-fatty acid esters ranging from pNP-acetate (C2) to pNP-stearate (C18) and films of PBSA, PBS, poly(ε-caprolactone), and poly(lactic acid). More... »

PAGES

7679-7688

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00253-012-4595-x

DOI

http://dx.doi.org/10.1007/s00253-012-4595-x

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1044094113

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/23224497


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