کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1383382 | 1500821 | 2016 | 6 صفحه PDF | دانلود رایگان |
• An apiose-based chromogenic probe was synthesized in good yield.
• β-d-Apiofuranosidase activity was detected in 15 out of 61 crude enzyme preparations
• Only enzyme preparations from aspergilli comprised the β-d-apiofuranosidase activity
4-Nitrophenyl β-d-apiofuranoside as a chromogenic probe for detection of β-d-apiofuranosidase activity was prepared in 61% yield from 2,3-isopropylidene-α,β-d-apiofuranose through a sequence of five reactions. The synthesis involves one regioselective enzymatic step—benzoylation of primary hydroxyl of 2,3-isopropylidene-α,β-d-apiofuranose catalysed by Lipolase 100T and stereoselective β-d-apiofuranosylation of p-nitrophenol using BF3⋅OEt2/Et3N. The product was used for screening of β-d-apiofuranosidase activity in 61 samples of crude commercial enzymes and plant materials. Fifteen enzyme preparations originating from different strains of genera Aspergillus display β-d-apiofuranosidase activity. The highest activity was found in Rapidase AR 2000 (78.27 U/g) and lyophilized Viscozyme L (64,36 U/g).
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Journal: Carbohydrate Research - Volume 430, 22 July 2016, Pages 48–53