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Oligopeptide patterns produced from Theobroma cacao L of various genetic origins
Author(s) -
Amin I,
Jinap S,
Jamilah B,
Harikrisna K,
Biehl B
Publication year - 2002
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.1098
Subject(s) - autolysis (biology) , pepstatin , oligopeptide , theobroma , biology , chemistry , biochemistry , protease , botany , peptide , enzyme
Abstract Acetone dry powder (AcDP) was prepared for six cocoa genotypes, namely Forastero (Amelonado type), Criollo, Trinitario, SCA 12, UIT1 and PBC 140. Hydrophobic oligopeptides were produced when autolysis of AcDP was carried out at pH 3.5. Comparative HPLC analysis showed that autolysis of AcDP from various genotypes revealed a similar pattern of oligopeptides. Most of the hydrophobic oligopeptides were not generated during autolysis of AcDP in the presence of protease inhibitor (Pepstatin A), indicating that the generation of these oligopeptides was due to the action of cocoa cotyledon aspartic endoprotease. This finding implies that the splitting action of aspartic endoprotease on vicilin (7S)‐class globulin (VCG) from various genotypes was the same. The information from the study provides additional evidence that there are no obvious differences in VCG composition between various genotypes. © 2002 Society of Chemical Industry