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Accession number;00A0301138
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| Title;Thermal Stability and Digestibility of .ALPHA.-Amylase Inhibitor from Phaseolus vulgaris cultivar Tora. |
| Author;
YOSHIKAWA HIDEKI
(Koka Women's Jr. Coll.)
KOTARU MAKOTO
(Koka Women's Jr. Coll.)
TANAKA CHIE
(Koka Women's Jr. Coll.)
IKEUCHI TSUNEO
(Koka Women's Jr. Coll.)
KAWABATA MAKOTO
(Koka Women's Jr. Coll.)
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Journal Title;Journal of the Japanese Society for Food Science and Technology
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Journal Code:F0895A
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ISSN:1341-027X
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VOL.47;NO.2;PAGE.158-162(2000)
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| Figure&Table&Reference;FIG.4, REF.20 |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;Tora bean .ALPHA.-amylase inhibitor(TAI) was a proteinaceous .ALPHA.-amylase inhibitor from Phaseolus vulgaris cultivar Tora, a common kidney bean in Japan, and it was active against pancreatic and salivary .ALPHA.-amylases. We investigated the behavior of this inhibitor during heat treatment and enzymatic digestion in order to evaluate the nutritional significance of kidney bean .ALPHA.-amylase inhibitor. The inhibition against pancreatic .ALPHA.-amylase increased with a rise in preincubation temperature from 25 to 45.DEG.C.. TAI was relatively stable in pH7.0 after 20min incubation at 80.DEG.C., while it was rapidly inactivated in pH3.0 and 5.0. Soaking of tora beans in water for 15h at 20.DEG.C. caused an decrease of soluble protein content, but hardly affect the inhibitory activity, while boiling treatment for 15min inactivated nearly 90% of the inhibitor. The inhibitor was quite resistant to the proteolysis by pepsin and trypsin, while it was relatively susceptible to hydrolysis by chymotrypsin and lost about 90% of the original activity during 2h digestion. (author abst.) |
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