EXTRACELLULAR LIGNINOLYTIC ENZYMES PRODUCTION BY Pleurotus eryngii ON AGROINDUSTRIAL WASTES


Akpinar M., ÖZTÜRK ÜREK R.

PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY, cilt.44, sa.8, ss.772-781, 2014 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 44 Sayı: 8
  • Basım Tarihi: 2014
  • Doi Numarası: 10.1080/10826068.2013.867870
  • Dergi Adı: PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.772-781
  • Anahtar Kelimeler: apricot, ligninolytic enzymes, Pleurotus eryngii, pomegranate, solid-state fermentation, MANGANESE PEROXIDASE PRODUCTION, LACCASE, FERMENTATION, OSTREATUS, KINETICS, CULTURES
  • Dokuz Eylül Üniversitesi Adresli: Evet

Özet

Pleurotus eryngii (DC.) Gillet (MCC58) was investigated for its ligninolytic ability to produce laccase (Lac), manganese peroxidase (MnP), aryl alcohol oxidase (AAO), and lignin peroxidase (LiP) enzymes through solid-state fermentation using apricot and pomegranate agroindustrial wastes. The reducing sugar, protein, lignin, and cellulose levels in these were studied. Also, the production of these ligninolytic enzymes was researched over the growth of the microorganism throughout 20 days, and the reducing sugar, protein, and nitrogen levels were recorded during the stationary cultivation at 28 +/- 0.5 degrees C. The highest Lac activity was obtained as 1618.5 +/- 25U/L on day 12 of cultivation using apricot. The highest MnP activity was attained as 570.82 +/- 15U/L on day 17 in pomegranate culture and about the same as apricot culture. There were low LiP activities in both cultures. The maximum LiP value detected was 16.13 +/- 0.8U/L in apricot cultures. In addition, AAO activities in both cultures showed similar trends up to day 17 of cultivation, with the highest AAO activity determined as 105.99 +/- 6.3U/L on day 10 in apricot cultures. Decolorization of the azo dye methyl orange was also achieved with produced ligninolytic enzymes by P. eryngii using apricot and pomegranate wastes.