[PDF][PDF] The effect of [Co (DH) 2 (An) 2] 2 [TiF6]· 3H2O coordination compound on polypeptide spectrum of amylolytic preparation from Aspergillus niger 33-19 CNMN …
From mycelial fungus Aspergillus niger 33-19 CNMN FD 02A cultivated on nutrient medium
supplemented with [Co (DH) 2 (An) 2] 2 [TiF6]· 3H2O coordination compound amylolytic
preparation with total α-amylase activity of 40042U/g and a specific activity of 131.3 U/mg
proteins was obtained. Through gel filtration and ion exchange chromatography enzyme
preparation was purified 7.8 fold with a yield of 13%. SDS-PAGE electrophoresis of purified
α-amylase revealed 2 polypeptide bands of 66 and 40.5 kDa identified as α-amylase …
supplemented with [Co (DH) 2 (An) 2] 2 [TiF6]· 3H2O coordination compound amylolytic
preparation with total α-amylase activity of 40042U/g and a specific activity of 131.3 U/mg
proteins was obtained. Through gel filtration and ion exchange chromatography enzyme
preparation was purified 7.8 fold with a yield of 13%. SDS-PAGE electrophoresis of purified
α-amylase revealed 2 polypeptide bands of 66 and 40.5 kDa identified as α-amylase …
THE EFFECT OF [Co(DH)2(An)2]2[TiF6].3H2O COORDINATION COMPOUND ON POLYPEPTIDE SPECTRUM OF AMYLOLYTIC PREPARATION FROM …
A CILOCI, C BIVOL, M STRATAN… - Annals of Oradea …, 2012 - search.ebscohost.com
From mycelial fungus Aspergillus niger 33-19 CNMN FD 02A cultivated on nutrient medium
supplemented with [Co (DH)< sub> 2(An)< sub> 2]< sub> 2[TiF< sub> 6]. 3H< sub> 2 O
coordination compound amylolytic preparation with total α-amylase activity of 40042U/g and
a specific activity of 131.3 U/mg proteins was obtained. Through gel filtration and ion
exchange chromatography enzyme preparation was purified 7.8 fold with a yield of 13%.
SDS-PAGE electrophoresis of purified α-amylase revealed 2 polypeptide bands of 66 and …
supplemented with [Co (DH)< sub> 2(An)< sub> 2]< sub> 2[TiF< sub> 6]. 3H< sub> 2 O
coordination compound amylolytic preparation with total α-amylase activity of 40042U/g and
a specific activity of 131.3 U/mg proteins was obtained. Through gel filtration and ion
exchange chromatography enzyme preparation was purified 7.8 fold with a yield of 13%.
SDS-PAGE electrophoresis of purified α-amylase revealed 2 polypeptide bands of 66 and …
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