Production of Endoglucanase by Exiguobacterium mexicanum OB24 Using Waste Melon Peels as Substrate

BALTACI M. Ö., ÖMEROĞLU M. A., ALBAYRAK Ş., Adiguzel G., ADIGÜZEL A.

ANAIS DA ACADEMIA BRASILEIRA DE CIENCIAS, cilt.94, 2022 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 94
  • Basım Tarihi: 2022
  • Doi Numarası: 10.1590/0001-3765202220220151
  • Dergi Adı: ANAIS DA ACADEMIA BRASILEIRA DE CIENCIAS
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Aerospace Database, Animal Behavior Abstracts, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, CAB Abstracts, Communication Abstracts, EMBASE, INSPEC, MEDLINE, Metadex, Veterinary Science Database, zbMATH, Directory of Open Access Journals, Civil Engineering Abstracts
  • Anahtar Kelimeler: Endoglucanase production, waste melon peel, Exiguobacterium mexicanum OB24, agricultural wastes, ENZYME-PRODUCTION, NITROGEN-SOURCE, OPTIMIZATION, RUMEN, FERMENTATION, BACTERIA, VALORISATION, PRETREATMENT, FRUIT
  • Atatürk Üniversitesi Adresli: Evet

Özet

Millions of tons of agricultural waste are produced globally every year. A practical solution to this global problem is to convert this waste into value-added products. In this study, endoglucanase enzyme production was carried out by using waste melon peels as a carbon source. To use this important resource, its stubborn structure must be broken down. Rumen bacteria are regarded as unique for this job. Therefore, firstly endoglucanase producing rumen bacteria was isolated and the bacteria with the best activity (OB24) were identified by molecular methods (165 rRNA gene squencing). As a result of the sequence analysis, it was determined that isolate belonged to Exiguobacterium mexicanum. Then, by optimizing the culture conditions, the enzyme production potential was increased. The optimal conditions were determined as 50 g/L MPP, 2g/L yeast extract, 60 h incubation time, pH: 6.0, and 40 degrees C temperature. Under optimized conditions the enzyme activity increased approximately 3.8-fold.