PURIFICATION, PROPERTIES AND COMPARISON OF INVERTASE, EXOINULINASES AND ENDOINULINASES OF ASPERGILLUS-FICUUM
PURIFICATION, PROPERTIES AND COMPARISON OF INVERTASE, EXOINULINASES AND ENDOINULINASES OF ASPERGILLUS-FICUUM
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DOI：
10.1007/bf00282143
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发表时间：
1987-04-01
影响因子：
5
通讯作者：
BARATTI, JC
中科院分区：
文献类型：
--
作者：
ETTALIBI, M;BARATTI, JC
One invertase (Inv), five exoinulinases (Exo I; II; III; IV; V) and three endoinulinases (Endo I; II; III) were isolated from a commercial inulinase preparation derived from Aspergillus ficuum using ammonium sulfate precipitation, ion exchange chromatography on DEAE-Sephacel and DEAE-Trisacryl, gel filtration on Ultrogel and Fast Protein Liquid Chromatography on a Mono Q column. The invertase (Inv) had a molecular weight of 84,000 and was much more active on sucrose than on inulin: the ratio of activity on inulin and sucrose (I/S ratio) was 0.01. The five exoinulinases show the same molecular weight of 74,000 and I/S ratios in the range 0.16-0.36. The three endoinulinases had molecular weight of 64,000 and I/S ratios in the range 0.86-2.92. All the .beta.-fructofuranosidases were glycoproteins with a high sugar content (from 22 to 41% w/w). A. ficuum is the first described organism containing the three activities: invertase, exo and endoinulinase.
