Isolation and identification of thermophilic cellulolytic yeast from cassava waste dump

dc.contributor.authorOnilude, A A
dc.contributor.authorAdekoya A O
dc.contributor.authorWakil, Sherifah Monilola
dc.contributor.authorFasiku, Samuel Adedayo
dc.contributor.authorJa'afaru, I M
dc.date.accessioned2026-06-28T17:04:24Z
dc.date.available2026-06-28T17:04:24Z
dc.date.issued2015
dc.description.abstractCellulase is an enzyme complex which breaks down cellulose to glucose. The need for economical, complete and fast industrial processes necessitates the use of very active starters able to operate at high temperature of production to degrade cheap nutrients most of which are cellulolytic; hence the search for thermophilic cellulolytic yeasts from the environment. Isolation and identification of thermophilic yeasts were made from the soil samples using standard procedures and obtained isolates were screened for cellulolytic enzymes production. The enzymes were characterised using different parameters such as temperature, pH, substrate concentrations, enzyme concentrations and metal ion concentrations. A total of seven thermophilic yeasts were isolated from cassava waste dump sites and identified as Torulopis sphaerica, Kloeckera apiculata, Pichia canadensis, Pichia species, Candida krusei, Candida utilis and Rodotorula rubra. They all had optimum growth at temperature and pH of 55ºC and 6.0 respectively. The optimum temperature and pH for cellulolytic activities ranged from 45-55ºC and 5-6 respectively. Cellulolytic activities increased with increase in the concentration of substrate, enzymes and metal ions.
dc.identifier.issn1119 - 7333
dc.identifier.urihttps://repository.acu.edu.ng/handle/123456789/1904
dc.language.isoen
dc.publisherJournal of Science Research
dc.relation.ispartofseries15
dc.subjectCellulolytic activities
dc.subjectthermophilic yeasts
dc.subjectsubstrate concentration
dc.subjection concentration
dc.titleIsolation and identification of thermophilic cellulolytic yeast from cassava waste dump
dc.typeArticle

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