บทคัดย่องานวิจัย

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Rhamnogalacturonase, alpha -galactosidase, and beta -galactosidase: potential roles in fruit softening.

Gross, K. C., Starrett, D. A. and Chen HueyJen

Acta Horticulturae Year: 1995 Issue: No. 398 Pages: 121-130 Ref: 43 ref.

1995

บทคัดย่อ

Rhamnogalacturonase, alpha -galactosidase, and beta -galactosidase: potential roles in fruit softening.

ABSTRACT :

 

alpha - and beta -Galactosidase were recently reported to solubilize tomato pectin in vitro. Both enzymes were extracted from the pericarp of tomato fruits. alpha -Galactosidase had an apparent MW of 44 kDa, a Km value of 317 micro M, a pI of 5.0 and a pH optimum of 5.5. The enzyme had a specific activity of 294 micro mol product min-1 mg-1 and was inhibited by alpha -D-galactose. Rhamnogalacturonase, recently identified, can degrade the pectic backbone and is potentially important in fruit softening and fungal decay. A method for assaying rhamnogalacturonase (RGase) activity is reported using alpha -rhamnosidase to hydrolyse unbranched terminal rhamnosyl residues from the oligomeric products. The released rhamnose is quantified by preparing its alditol acetate derivative and analysing by gas chromatography. Using this assay, RGase activity was detected in tomatoes, apples and grapes as well as in Botrytis cinerea, an important postharvest pathogen.