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Aryl‐Glycosidase Activities in Germinating Maize
Author(s) -
Biely Peter,
Ahlgren Jeffrey A.,
Leathers Timothy D.,
Greene Richard V.,
Cotta Michael A.
Publication year - 2003
Publication title -
cereal chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.558
H-Index - 100
eISSN - 1943-3638
pISSN - 0009-0352
DOI - 10.1094/cchem.2003.80.2.144
Subject(s) - chemistry , glycoside hydrolase , enzyme , xylanase , isoelectric point , biochemistry , hydrolysis , germination , isoelectric focusing , beta glucosidase , xylose , specific activity , enzyme assay , botany , biology , fermentation
Soluble protein extracts of germinating maize seedlings exhibited a limited ability to hydrolyze purified xylans, and specific assays were unable to confirm the presence of endo‐β‐1,4‐xylanase activity. However, extracts contained a variety of aryl‐glycosidase activities, including β‐glucosidase, β‐xylosidase, and α‐ l ‐arabinofuranosidase. These activities peaked in three‐ to four‐day seedlings and were particularly concentrated in shoot and root tissues. Maximal levels of β‐glucosidase were two orders of magnitude greater than those of β‐xylosidase or α‐ l ‐arabinofuranosidase. Isoelectric focusing gels revealed multiple forms of these enzymes. The principal β‐glucosidase and α‐ l ‐arabinofuranosidase protein species were clustered at pI 4.8–4.9 and pI 5.8–6.0, respectively. β‐Xylosidase activity appeared to be associated with both of these enzymes, and no evidence was obtained for a distinct β‐xylosidase.