Partial purification and biochemical characterization of an extremely thermo- and pH-stable esterase with great substrate affinity

Đang chuẩn bị liên kết để tải về tài liệu:
Partial purification and biochemical characterization of an extremely thermo- and pH-stable esterase with great substrate affinity

Mạnh Cương 64 9 pdf

Presence of 10% (v/v) acetonitrile in the reaction medium indicated that purified enzyme was strongly inhibited. It was also detected that some metal ions affected enzyme activity at different rates. As a result, it was observed that esterase from Geobacillus sp. DF20 has extreme temperature and pH stabilities. Therefore, the stability and Km value of the enzyme make this study interesting when compared with the literature. |

Đang chuẩn bị liên kết để tải về tài liệu:
Partial purification and biochemical characterization of an extremely thermo- and pH-stable esterase with great substrate affinity

Screening and partial purification of L-Asparaginase from the bacteria isolated from soil samples

Partial purification and biochemical characterization of an extremely thermo- and pH-stable esterase with great substrate affinity

Optimization for production and partial purification of laccase from ash gourd peels

Optimization of culture conditions using one-factor-at-time methodology and partial purification of amylase from aspergillus niger of DTO: H5 under solid state fermentation

Isolation, screening, optimization of cultural conditions of submerged fermentation and partial purification of alkaline chitinase enzyme from Fusarium sp.

Partial purification of hen egg white lysozyme by ethanol precipitation method and determination of the thermal stability of its lyophilized form

Partial purification and characterization of cellulases from digestive tracts of the African giant snail (Achatina achatina)

Partial purification of intestinal triglyceride lipase from Cyprinion macrostomus Heckel, 1843 and effect of Ph on enzyme activity

Purification and partial characterization of intracellular fructosyltransferase from a novel strain of Aureobasidium pullulans

Partial purification and characterization of proteases from the visceral waste of Indian major carp, Labeo Rohita (Hamilton, 1822)

Đang chuẩn bị liên kết để tải về tài liệu: Partial purification and biochemical characterization of an extremely thermo- and pH-stable esterase with great substrate affinity

Screening and partial purification of L-Asparaginase from the bacteria isolated from soil samples

Partial purification and biochemical characterization of an extremely thermo- and pH-stable esterase with great substrate affinity

Optimization for production and partial purification of laccase from ash gourd peels

Optimization of culture conditions using one-factor-at-time methodology and partial purification of amylase from aspergillus niger of DTO: H5 under solid state fermentation

Isolation, screening, optimization of cultural conditions of submerged fermentation and partial purification of alkaline chitinase enzyme from Fusarium sp.

Partial purification of hen egg white lysozyme by ethanol precipitation method and determination of the thermal stability of its lyophilized form

Partial purification and characterization of cellulases from digestive tracts of the African giant snail (Achatina achatina)

Partial purification of intestinal triglyceride lipase from Cyprinion macrostomus Heckel, 1843 and effect of Ph on enzyme activity

Purification and partial characterization of intracellular fructosyltransferase from a novel strain of Aureobasidium pullulans

Partial purification and characterization of proteases from the visceral waste of Indian major carp, Labeo Rohita (Hamilton, 1822)

Đang chuẩn bị liên kết để tải về tài liệu:
Partial purification and biochemical characterization of an extremely thermo- and pH-stable esterase with great substrate affinity