ISHS Acta Horticulturae 517: XXV International Horticultural Congress, Part 7: Quality of Horticultural Products
PURIFICATION AND CHARACTERIZATION OF α-L-ARABINOFURANOSI-DASE FROM JAPANESE PEAR FRUIT |
| Authors: | A. Tateishi, H. Inoue |
| Keywords: | α-L-arabinofuranosidase, Japanese pear, ripening, β-galactosidase |
| Abstract:
To find out whether  -L-arabinofuranosidase and b-galactosidase play important roles during Japanese pear fruit softening, the enzyme activities were assayed in some Japanese cultivar; Shinsui, Kousui, Housui and Niitaka. -L-Arabinofuranosidase activity increased during ripening in their Japanese cultivar.
The increase of activity earlier in the early ripening cultivar.
It reflects that physiological stage of ripening in each cultivar.
The enzyme plays an important role in fruit softening with ripening.  -Galactosidase activity began to increase after the optimum harvest date.
The enzyme may involve in cell wall degradation with overripening.
Alternatively, -galactosidase isoform activities may be overlap each other.
In order to elucidate the chage of softening related -galactosidase activities, it is necessary to assay separately. -L-arabinofuranosidase was solubilized in the presence of both NaCl and Triton X-100. About 250% of cell wall-bound -L-arabinofuranosidase activity was recovered.
The result indicates that NaCl and Triton X-100 effectively solubilized -L-arabinofuranosidase from cell wall.
In addition, the enzyme may be stabilized by Triton X-100 under high salt concentration.
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