• Corpus ID: 85729449

Production and partial purification of extracellular lipase produced by a novel yeast strain Candida odintsovae TY42 (Yeni bir maya suşu olan Candida odintsovae TY42 tarafindan üretilen hücre dişi lipazin üretimi ve kismi saflaştirilmasi)

@inproceedings{Kartal2014ProductionAP,
  title={Production and partial purification of extracellular lipase produced by a novel yeast strain Candida odintsovae TY42 (Yeni bir maya suşu olan Candida odintsovae TY42 tarafindan {\"u}retilen h{\"u}cre dişi lipazin {\"u}retimi ve kismi saflaştirilmasi)},
  author={Funda Kartal and H{\"u}sniye Tansel Yalçin},
  year={2014}
}

• Funda Kartal, Hüsniye Tansel Yalçin
• Published 2014
• Biology

Objective: Nowadays, in most of industrial technology, especially biotechnological processes, use of enzymes is increasingly widespread. With respect to discovery of new enzymes, one of the most successful methods is isolation of microorganisms from natural habitats. Therefore, in this research, we aimed to isolate and characterize lipase producing yeasts and purify the extracellular lipase produced by a novel yeast strain Candida odintsovae TY42. Methods: The yeasts used in the study were isolated from olive oils and identified based on sequence analyses of ITS1-5.8S rRNA-ITS2 and D1/D2 domain of 26S rRNA. The optimal nutritional and physicochemical conditions were determined by investigating the effects of initial pH and temperature and different carbon sources on enzyme production in basal medium. The lipase was purified by ammonium sulfate and acetone precipitation and anion exchange chromatography. Results: Three lipase producing yeast isolates were obtained from olive oils produced in Aegean region. The sequencing of rRNA regions revealed that novel strains, TY17, TY42 and TY54 identified as Candida odintsovae. C. odintsovae TY42 showed higher lipase activity and therefore, the yeast was selected for further investigations. The maximum lipase production was achieved in a medium containing fish oil after 144 h of incubation. The lipase was purified 12.8 fold. The molecular weight of the purified lipase was estimated to be about 39 kDa.