Anti-homogalacturonan antibodies: A way to explore the effect of processing on pectin in fruits and vegetables?

Towards a better understanding of the pectin structure–function relationship in broccoli during processing: Part I—macroscopic and molecular analyses

“…In the second part of the study, this information is complemented by pectin analysis using anti-HG antibodies (see complementary publication by Christiaens et al), entailing in situ (microscopy) and ex situ (immuno-dot assays) analyses. This approach has only recently been introduced to study process-induced changes in pectin's structure in fruits and vegetables (Christiaens et al, 2011) and is one of the few techniques available for analysis of the intact cell wall matrix. In combination with results from the current part of the study, it provides a detailed image of changes in the HG component of pectin during (pre)processing of plant tissues, which improves our understanding of the pectin structure-function relationship.…”

Towards a better understanding of the pectin structure–function relationship in broccoli during processing: Part II — Analyses with anti-pectin antibodies

“…We recently introduced the use of anti-HG antibodies to study process-induced changes in pectin structure in fruits and vegetables (Christiaens et al, 2011). In fact, the current study is one of the first studies in the context of food processing that actually complements the ex situ pectin-characterisation methods with in situ pectin visualisation by means of anti-pectin antibodies.…”

“…Several recent advances in pectin analysis now make it possible to complement these findings with precise information obtained by in situ visualisation of pectin (Christiaens et al, 2011;Willats et al, 2006). A number of monoclonal antibodies towards different pectic structures have become available, which allow the precise localisation of defined structural pectic domains in intact plant cell walls.…”

“…Of particular interest for food technologists are a set of antibodies that bind to HG domains of pectin, including JIM5, JIM7, LM18, LM19, LM20, PAM1, and 2F4 (Table 1). Knowledge on the binding specificities of these antibodies is at hand: antibodies LM18 and LM19 need a stretch of unesterified GalA residues for recognition, while methyl-esterified residues are required for the binding of LM20 (Christiaens et al, 2011;Verhertbruggen, Marcus, Haeger, Ordaz-Ortiz, & Knox, 2009). In contrast, the epitope of JIM5 contains both methyl-esterified and non-methyl-esterified GalA residues (Willats et al, 2000).…”

“…In contrast, the epitope of JIM5 contains both methyl-esterified and non-methyl-esterified GalA residues (Willats et al, 2000). JIM7 can be used as a general antipectin probe as it recognises HG with very diverse degrees and patterns of methyl-esterification (Christiaens et al, 2011;Willats et al, 2000). PAM1, on the other hand, is a much more 'specific' antibody since it only binds to long blocks of approximately 30 non-esterified GalA residues (Willats, Gilmartin, Mikkelsen, & Knox, 1999).…”