Production, characteristics and applications of the cell-bound phytase of Pichia anomala.
Among several yeasts isolated from dried flowers of Woodfordia fruticosa, Pichia anomala produced a high titre of cell-bound phytase. The optimization of fermentation variables led to formulation of media and selection of cultural variables that supported enhanced phytase production. The enzyme productivity was very high in fed batch fermentation in air-lift fermentor as compared to that in stirred tank fermentor. Amelioration in the cell-bound phytase activity was observed when yeast cells were permeabilized with Triton-X-100. The enzyme is thermostable and acid stable with broad substrate specificity, the characteristics that are desirable for enzymes to be used in the animal feed industry. The phytase-encoding gene was cloned and sequenced. The 3D structure of the enzyme was proposed by comparative modeling using phytase of Debaryomyces occidentalis (50% sequence identity) as template. When broiler chicks, and fresh water and marine fishes were fed with the feed supplemented with yeast biomass containing phytase, improvement in growth and phosphorus retention, and decrease in the excretion of phosphorus in the faeces were recorded. The cell-bound phytase of P. anomala could effectively dephytinize wheat flour and soymilk.
Vohra
Ashima
A
Department of Microbiology, University of Delhi South Campus, New Delhi 110021, India.
Kaur
Parvinder
P
Satyanarayana
T
T
D010832:6-Phytase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003001:Cloning, Molecular; D003470:Culture Media / Q000737:chemistry; D019587:Dietary Supplements; D004795:Enzyme Stability; D005285:Fermentation; D008958:Models, Molecular; D010843:Pichia / Q000201:enzymology* / Q000254:growth & development; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity
D003470:Culture Media; D010832:6-Phytase