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Characterization of a grape class IV chitinase.

ABSTRACT: A chitinase was purified from Vitis vinifera Manzoni Bianco grape juice and characterized. On the basis of proteomic analysis of tryptic peptides, a significant match identified the enzyme as a type IV grape chitinase previously found in juices of other V. vinifera varieties. The optimal pH and temperature for activity toward colloidal chitin were found to be 6 and 30 °C, respectively. The enzyme was found to hydrolyze chitin and oligomers of N-acetylglucosamine, generating N,N'-diacetylchitobiose and N-acetylglucosamine as products, but was inactive toward N,N'-diacetylchitobiose. The enzyme exhibited both endo- and exochitinase activities. Because yeast contains a small amount of chitin in the cell wall, the possibility of growth inhibition was tested. At a concentration and pH expected in ripe grapes, no inhibition of wine yeast growth by the chitinase was observed.

SUBMITTER: Vincenzi S

PROVIDER: S-EPMC4216234 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature

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Characterization of a grape class IV chitinase.

Vincenzi Simone S Bierma Jan J Wickramasekara Samanthi I SI Curioni Andrea A Gazzola Diana D Bakalinsky Alan T AT

Journal of agricultural and food chemistry 20140603 24

A chitinase was purified from Vitis vinifera Manzoni Bianco grape juice and characterized. On the basis of proteomic analysis of tryptic peptides, a significant match identified the enzyme as a type IV grape chitinase previously found in juices of other V. vinifera varieties. The optimal pH and temperature for activity toward colloidal chitin were found to be 6 and 30 °C, respectively. The enzyme was found to hydrolyze chitin and oligomers of N-acetylglucosamine, generating N,N'-diacetylchitobio ...[more]

PMID: 24845689

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