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Structure and stability of alpha-amylase inhibitors from the seeds of Shirohanamame (Phaseolus coccineus L.), Murasakihanamame (Phaseolus coccineus L.), Toramame (Phaseolus vulgaris L.) and Uzuramame (Phaseolus vulgaris L.)



Structure and stability of alpha-amylase inhibitors from the seeds of Shirohanamame (Phaseolus coccineus L.), Murasakihanamame (Phaseolus coccineus L.), Toramame (Phaseolus vulgaris L.) and Uzuramame (Phaseolus vulgaris L.)



Nippon Shokuhin Kagaku Kogaku Kaishi 53(10): 534-541



The structure and stability of four a-amylase inhibitors (TAT, UAI, MAI-2 and SAI-2) from Toramame (Phaseolus vulgaris L.), Uzuramame (Phaseolus vulgaris L.), Murasakihanamame (Phaseolus coccineus L.) and Shirohanamame (Phaseolus coccineus L.) were examined. The amino acid sequence of SAI-2 was the same as the known sequence for MAI-2, but was slightly different from that of TAT and UAI. The sugar chain composition of SAI-2 was remarkably different from that of MAI-2. Thermal stability at pH 5.0, 70 degrees C indicated that SAI-2 and MAI-2 have markedly similar stabilities. Likewise, TAT and UAI, which also had identical amino acid sequences, exhibited markedly similar stabilities.However, SAI-2 and MAI-2 were more stable than TAT and UAI. These results suggest that thermal stability of a-amylase inhibitors depends on a few amino acid substitutions in their primary structures.

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Accession: 012889623

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DOI: 10.3136/nskkk.53.534


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Structure and stability of alpha-amylase inhibitors from the seeds of Shirohanamame (Phaseolus coccineus L.), Murasakihanamame (Phaseolus coccineus L.), Toramame (Phaseolus vulgaris L.) and Uzuramame (Phaseolus vulgaris L.). Journal of the Japanese Society for Food Science and Technology-Nippon 53(10): 534-541, 2006

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