A highly active esterase from Lactobacillus helveticus hydrolyzes chlorogenic acid in sunflower meal to prevent chlorogenic acid induced greening in sunflower protein isolates

Verde, Christine Lo; Pepra-Ameyaw, Nana Baah; Drucker, Charles T.; Okumura, Tracie L S; Lyon, Katherine; Muniz, Julia C.; Sermet, Chloe S.; Senger, Lilian M. Were; Owens, Cedric P.

doi:10.1016/j.foodres.2022.111996

Cited by 7 publications

(18 citation statements)

References 48 publications

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“…The spectra are indistinguishable, indicating that esterase treatment does not alter the structure of lipids, proteins, or carbohydrates within the cookie. These data confirm previous results that L. helveticus CGA esterase is specific and does not act on biomolecules other than CGA to a noticeable degree (Lo Verde et al., 2022).…”

Section: Resultssupporting

confidence: 92%

“…Enzymatic treatment is being increasingly used to enhance the properties of side streams and create upcycled ingredients (Hoang et al., 2022; Nguyen et al., 2021). The physical properties of CGA esterase would make this enzyme well suited for commercial application since it is stable and displays comparable activity similar to other enzymes that are currently used in the food industry (Lo Verde et al., 2022).…”

Section: Discussionmentioning

confidence: 99%

“…Lactobacillus helveticus CGA esterase was expressed and purified according to procedures described in Lo Verde et al. (2022) with the modification that the enzyme was dialyzed into 20 mM potassium phosphate buffer, pH 8.0 prior to being used in baking as phosphate salts are generally recognized as safe for human consumption (21CFR182, n.d.). After being dialyzed, CGA esterase was sterile‐filtered using a 0.2 µm filter.…”

Section: Methodsmentioning

confidence: 99%

“…These methods, however, have limited effectiveness, are costly, or remove beneficial phenolics from the flour. Our group recently demonstrated that a recombinantly expressed CGA esterase from Lactobacillus helveticus rapidly hydrolyzes CGA into caffeic acid (CA) and quinic acid (Lo Verde et al., 2022). CGA esterase treatment prevented greening in alkaline‐extracted sunflower protein isolates (Lo Verde et al., 2022) and cookies made with SFF (Pepra‐Ameyaw et al., 2022).…”

Section: Introductionmentioning

confidence: 99%

“…Our group recently demonstrated that a recombinantly expressed CGA esterase from Lactobacillus helveticus rapidly hydrolyzes CGA into caffeic acid (CA) and quinic acid (Lo Verde et al., 2022). CGA esterase treatment prevented greening in alkaline‐extracted sunflower protein isolates (Lo Verde et al., 2022) and cookies made with SFF (Pepra‐Ameyaw et al., 2022). While this demonstrated that SFF can be used to produce non‐green cookies while retaining beneficial phenolics, the questions of whether SFF cookies are appealing to consumers and whether they would accept enzymatically treated SFF cookies were left unanswered.…”

Section: Introductionmentioning

confidence: 99%

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Hydrolysis of chlorogenic acid in sunflower flour increases consumer acceptability of sunflower flour cookies by improving cookie color

Verde

Pacioles

Paterson

et al. 2023

Journal of Food Science

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Sunflower meal, a byproduct of sunflower oil pressing, is not commonly used in alkaline baking applications. This is because chlorogenic acid, the main phenolic antioxidant in sunflower seeds, reacts with protein, giving the baked product a green discoloration. Our group previously demonstrated that a chlorogenic acid esterase from Lactobacillus helveticus hydrolyzes chlorogenic acid in sunflower dough cookie formulations, resulting in cookies that were brown instead of green. This study presents a sensory analysis to determine the acceptability of enzymatically upcycled sunflower meal as an alternative protein source for those allergic to meals from legumes or tree nuts. We hypothesized that the mechanism of esterase‐catalyzed chlorogenic acid breakdown does not influence the cookies’ sensory properties other than color and that consumers would prefer treated, brown cookies over non‐treated cookies. Cookies made from sunflower meal were presented under green lights to mask color and tested by 153 panelists. As expected, the sensory properties (flavor, smell, texture, and overall acceptability) of the treated and non‐treated cookies were not statistically different. These results corroborate proximate analysis, which demonstrated that there was no difference between enzymatically treated and non‐treated cookies other than color and chlorogenic acid content. After the cookie color was revealed, panelists strongly preferred the treated cookies with 58% indicating that they “probably” or “definitely” would purchase the brown cookies, whereas only 5.9% would buy green, non‐treated cookies. These data suggest that esterase‐catalyzed breakdown of chlorogenic acid represents an effective strategy to upcycle sunflower meal for baking applications. Practical Application Sunflower meal is currently used as animal fodder or discarded. A major factor preventing sunflower meal use is its high chlorogenic acid content, which causes a green discoloration of baked goods made from sunflower meals under alkaline conditions. This study presents a sensory analysis in which panelists evaluate cookies made with sunflower flour that was treated with an esterase that breaks down chlorogenic acid. The results show that enzymatic treatment prevents greening and that panelists strongly prefer esterase‐treated, non‐green cookies, thus demonstrating the feasibility of utilizing sunflower flour in baking applications.

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Section: Resultssupporting

confidence: 92%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Hydrolysis of chlorogenic acid in sunflower flour increases consumer acceptability of sunflower flour cookies by improving cookie color

Verde

Pacioles

Paterson

et al. 2023

Journal of Food Science

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The structure of a Lactobacillus helveticus chlorogenic acid esterase and the dynamics of its insertion domain provide insights into substrate binding

Omori,

Drucker,

Okumura

et al. 2023

FEBS Letters

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Chlorogenic acid esterases (ChlEs) are a useful class of enzymes that hydrolyze chlorogenic acid (CGA) into caffeic and quinic acids. ChlEs can break down CGA in foods to improve their sensory properties and release caffeic acid in the digestive system to improve the absorption of bioactive compounds. This work presents the structure, molecular dynamics, and biochemical characterization of a ChlE from Lactobacillus helveticus (Lh). Molecular dynamics simulations suggest that substrate access to the active site of LhChlE is modulated by two hairpin loops above the active site. Docking simulations and mutational analysis suggest that two residues within the loops, Gln145 and Lys164, are important for CGA binding. Lys164 provides a slight substrate preference for CGA, whereas Gln145 is required for efficient turnover. This work is the first to examine the dynamics of a bacterial ChlE and provides insights on substrate binding preference and turnover in this type of enzyme.

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A surface multiple imprinting layers membrane with well-oriented recognition sites for selective separation of chlorogenic acid from Ficus carica L.

Luo,

Tian,

Ahmad

et al. 2024

Food Chemistry

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A highly active esterase from Lactobacillus helveticus hydrolyzes chlorogenic acid in sunflower meal to prevent chlorogenic acid induced greening in sunflower protein isolates

Cited by 7 publications

References 48 publications

Hydrolysis of chlorogenic acid in sunflower flour increases consumer acceptability of sunflower flour cookies by improving cookie color

Hydrolysis of chlorogenic acid in sunflower flour increases consumer acceptability of sunflower flour cookies by improving cookie color

The structure of a Lactobacillus helveticus chlorogenic acid esterase and the dynamics of its insertion domain provide insights into substrate binding

A surface multiple imprinting layers membrane with well-oriented recognition sites for selective separation of chlorogenic acid from Ficus carica L.

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