Production studies, purification,and characterization of amylolytic enzyme from saccharomycopsis fibuligera 2074 isolated from Philippine bubod starter /
Bullo, Lani Lee Rigor.
Production studies, purification,and characterization of amylolytic enzyme from saccharomycopsis fibuligera 2074 isolated from Philippine bubod starter / Lani Lee Rigor Bullo. - 2009 - 73 leaves.
Thesis (BS Food Technology) -- University of the Philippines Mindanao, 2009
Saccharomycopsis fibuligera 2074 was identified to produce the highest extracellular raw starch-digesting amylase among eight amylolytic bubod isolates screened. Maximum growth and amylase production was obtained from 36-hour culture using 1% raw sago starch as the major carbon source. The enzyme was purified 2.56- fold, with a specific activity of 180.49 U/mg after DEAE-cellulose anion-exchange column chromatography. Amylase activity was optimum at pH of 6 and at 400C, Although the enzyme was inhibited by CU2+, Zn2+ and Al3+, it was activated by Ca2+, Fe3+, Ba2+, phenylmethylsulfonyl fluoride and ethylenediaminetetraacetic acid. On the other hand, iodoacetic acid K+, Cd2+, and Mg2+, showed no significant effect on amylase activity. The purified amylase showed interesting properties necessary for industrial application.
Amylases.
Bubod yeasts.
Amylase isolation.
Enzyme characterization.
Enzyme production.
Protein purification.
Saccharomycopsis fubuligera 2074.
Starch-digesting amylase.
Hydrolysis.
Starch.
Undergraduate Thesis --FST200,
Production studies, purification,and characterization of amylolytic enzyme from saccharomycopsis fibuligera 2074 isolated from Philippine bubod starter / Lani Lee Rigor Bullo. - 2009 - 73 leaves.
Thesis (BS Food Technology) -- University of the Philippines Mindanao, 2009
Saccharomycopsis fibuligera 2074 was identified to produce the highest extracellular raw starch-digesting amylase among eight amylolytic bubod isolates screened. Maximum growth and amylase production was obtained from 36-hour culture using 1% raw sago starch as the major carbon source. The enzyme was purified 2.56- fold, with a specific activity of 180.49 U/mg after DEAE-cellulose anion-exchange column chromatography. Amylase activity was optimum at pH of 6 and at 400C, Although the enzyme was inhibited by CU2+, Zn2+ and Al3+, it was activated by Ca2+, Fe3+, Ba2+, phenylmethylsulfonyl fluoride and ethylenediaminetetraacetic acid. On the other hand, iodoacetic acid K+, Cd2+, and Mg2+, showed no significant effect on amylase activity. The purified amylase showed interesting properties necessary for industrial application.
Amylases.
Bubod yeasts.
Amylase isolation.
Enzyme characterization.
Enzyme production.
Protein purification.
Saccharomycopsis fubuligera 2074.
Starch-digesting amylase.
Hydrolysis.
Starch.
Undergraduate Thesis --FST200,