Enzymatic synthesis of p-nitrophenyl alpha-maltoheptaoside by transglycosylation of maltohexaose-forming amylase.

Article abstract of DOI:10.1080/00021369.1990.10869998

An extracellular maltohexaose-forming amylase [EC 3.2.1.98] from Klebsiella pneumoniae mutant is a normal hydrolytic enzyme that hydrolyzes short-chain amylose (DP = 23) to give about 40% maltohexaose. Transglycosylation from maltoheptaose to the 4-position of p-nitrophenyl alpha-glucoside was efficiently induced through the use of maltohexaose-forming amylase in an aqueous methanol solution. The enzyme specifically produced p-nitrophenyl alpha-maltoheptaoside (13% of the p-nitrophenyl alpha-glucoside) from maltoheptaose as a donor and p-nitrophenyl alpha-glucoside as an acceptor. The yield of p-nitrophenyl alpha-maltoheptaoside depended on the concentration of methanol solvent, the pH, and temperature. Furthermore, the use of the aqueous methanol system in the reaction not only improved the solubility of p-nitrophenyl alpha-glucoside but also greatly increased the formation of p-nitrophenyl alpha-maltoheptaoside, which is a useful substrate for assay of human amylase in serum and urine.

Full text of DOI:10.1080/00021369.1990.10869998

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Enzymatic Synthesis of p-
Nitrophenyl α-Maltoheptaoside by
Transglycosylation of Maltohexaose-
forming Amylase
Koichi Ogawaa, Osamu Uejimaa, Teruo Nakakukia, Taichi Usuiab
Keiji Kainumaac
&
a Research Laboratory, Nihon Shokuhin Kako Co., Ltd., 30, Tajima,
Fuji, Shizuoka 417, Japan
b Department of Agricultural Chemistry, Faculty of Agriculture,
Shizuoka University, Shizuoka 422, Japan
c Biotechnology Division, Ministry of Agriculture, Forestry and
Fisheries, 1-2-1, Kasumigaseki, Chiyoda-ku, Fokyo 100, Japan
Published online: 08 Sep 2014.
To cite this article: Koichi Ogawa, Osamu Uejima, Teruo Nakakuki, Taichi Usui & Keiji Kainuma
(1990) Enzymatic Synthesis of p-Nitrophenyl α-Maltoheptaoside by Transglycosylation of
Maltohexaose-forming Amylase, Agricultural and Biological Chemistry, 54:3, 581-586
To link to this article: http://dx.doi.org/10.1080/00021369.1990.10869998
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