Synthesis of 2-O-a-D-glucopyranosyl L-ascorbic acid by cyclomaltodextrin glucanotransferase from bacillus sp.
Cyclomaltodextrin glucanotransferase (CGTase) [EC 2.4.1.19] was found to catalyze the transglycosylation from α-cyclodextrin (α-CD) to l-ascorbic acid (AA). A main product formed by this reaction was identified as 2-O-α-d-glucopyranosyl l-ascorbic acid (AA-2G) with the enzymatic hydrolysis and ultra...
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Online Access: | http://eprints.utm.my/id/eprint/2794/1/74184.pdf http://eprints.utm.my/id/eprint/2794/ http://www.tandfonline.com/doi/abs/10.1080/00021369.1991.10870856 |
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my.utm.27942017-06-15T03:06:00Z http://eprints.utm.my/id/eprint/2794/ Synthesis of 2-O-a-D-glucopyranosyl L-ascorbic acid by cyclomaltodextrin glucanotransferase from bacillus sp. Abd. Rahman, Roshanida TP Chemical technology Cyclomaltodextrin glucanotransferase (CGTase) [EC 2.4.1.19] was found to catalyze the transglycosylation from α-cyclodextrin (α-CD) to l-ascorbic acid (AA). A main product formed by this reaction was identified as 2-O-α-d-glucopyranosyl l-ascorbic acid (AA-2G) with the enzymatic hydrolysis and ultraviolet absorption spectra using standard AA-2G. A series of maltooligosaccharide substituted 2-O-derivatives of AA were also detected by HPLC. These were thoroughly hydrolized to AA-2G and glucose by treatment with glucoamylase [EC 3.2.1.3]. A large amount of AA-2G was prepared with 500 g of AA and 1000 g of α-CD. Two hundred and fifty grams of purified AA-2G, the content of which was 97%, was obtained through enzyme reactions and purification with HPLC using an ion-exchange resin. Universiti Teknologi Malaysia 2006-03-31 Monograph NonPeerReviewed application/pdf en http://eprints.utm.my/id/eprint/2794/1/74184.pdf Abd. Rahman, Roshanida (2006) Synthesis of 2-O-a-D-glucopyranosyl L-ascorbic acid by cyclomaltodextrin glucanotransferase from bacillus sp. Project Report. Universiti Teknologi Malaysia, Skudai, Johor. (Unpublished) http://www.tandfonline.com/doi/abs/10.1080/00021369.1991.10870856 |
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TP Chemical technology Abd. Rahman, Roshanida Synthesis of 2-O-a-D-glucopyranosyl L-ascorbic acid by cyclomaltodextrin glucanotransferase from bacillus sp. |
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Cyclomaltodextrin glucanotransferase (CGTase) [EC 2.4.1.19] was found to catalyze the transglycosylation from α-cyclodextrin (α-CD) to l-ascorbic acid (AA). A main product formed by this reaction was identified as 2-O-α-d-glucopyranosyl l-ascorbic acid (AA-2G) with the enzymatic hydrolysis and ultraviolet absorption spectra using standard AA-2G. A series of maltooligosaccharide substituted 2-O-derivatives of AA were also detected by HPLC. These were thoroughly hydrolized to AA-2G and glucose by treatment with glucoamylase [EC 3.2.1.3]. A large amount of AA-2G was prepared with 500 g of AA and 1000 g of α-CD. Two hundred and fifty grams of purified AA-2G, the content of which was 97%, was obtained through enzyme reactions and purification with HPLC using an ion-exchange resin. |
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Monograph |
author |
Abd. Rahman, Roshanida |
author_facet |
Abd. Rahman, Roshanida |
author_sort |
Abd. Rahman, Roshanida |
title |
Synthesis of 2-O-a-D-glucopyranosyl L-ascorbic acid by cyclomaltodextrin glucanotransferase from bacillus sp. |
title_short |
Synthesis of 2-O-a-D-glucopyranosyl L-ascorbic acid by cyclomaltodextrin glucanotransferase from bacillus sp. |
title_full |
Synthesis of 2-O-a-D-glucopyranosyl L-ascorbic acid by cyclomaltodextrin glucanotransferase from bacillus sp. |
title_fullStr |
Synthesis of 2-O-a-D-glucopyranosyl L-ascorbic acid by cyclomaltodextrin glucanotransferase from bacillus sp. |
title_full_unstemmed |
Synthesis of 2-O-a-D-glucopyranosyl L-ascorbic acid by cyclomaltodextrin glucanotransferase from bacillus sp. |
title_sort |
synthesis of 2-o-a-d-glucopyranosyl l-ascorbic acid by cyclomaltodextrin glucanotransferase from bacillus sp. |
publisher |
Universiti Teknologi Malaysia |
publishDate |
2006 |
url |
http://eprints.utm.my/id/eprint/2794/1/74184.pdf http://eprints.utm.my/id/eprint/2794/ http://www.tandfonline.com/doi/abs/10.1080/00021369.1991.10870856 |
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1643643657519104000 |
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13.18916 |