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KMID : 0903519870300040305
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology
1987 Volume.30 No. 4 p.305 ~ p.310
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Comparison of Soybean and Sweet Potato β - Amylases
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김영휘/Kim, Young Hui
김준평/Mikami, Bunzo/Majima.Keiichi/Morita, Yuhei/Kim, Jun Pyong
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Abstract
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The enzymatic properties of β-amylase from soybean and sweet potato here compared. The sweet potato enzyme consists of four identical subunits whereas soybean enzyme has no subunits structure. In the denatured state, both enzymes exhibited the same molecular weight on SDS-gel electrophoresis and on gel-filtration analysis. The spectra of circular dichroism revealed that both enzyme have almost same secondary structure but the environment of aromatic side chains are different. The chemical cleavage of soybean and sweet potato β-amylases at cysteine residues and methionine residues demonstrated the homology of amino acid sequence between the enzymes. The similarity between soybean and sweet potato β-amylase was also revealed by immunological method. The antibody for soybean enzyme inhibited the activity of sweet potato enzyme but it did not inhibit the activity of wheat, barley and Japanese-rad-dish β-amylases.
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