Impact of aqualysin 1 peptidase from Thermus aquaticus on molecular scale changes in the wheat gluten network during bread baking

Verbauwhede, Annelien E.; Lambrecht, Marlies A.; Fierens, Ellen; Shegay, Oksana; Brijs, Kristof; Delcour, Jan A.

doi:10.1016/j.foodchem.2019.05.161

Cited by 7 publications

(11 citation statements)

References 24 publications

(44 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Reactions among gluten proteins occur from about 50°C onwards in bread baking (Verbauwhede, Lambrecht, Fierens, et al, 2019) and affect the gluten microstructure (Verbauwhede, Lambrecht, Jekle, et al, 2019). We reasoned that to understand the relevance of these changes for bread macroscopic properties, it would be ideal to inactivate Aq1 during mixing and fermentation and allow activity during baking from about 50°C, 60°C, or 70°C onwards.…”

Section: Resultsmentioning

confidence: 99%

“…Aq1 activity was measured as in Verbauwhede, Lambrecht, Fierens, et al (2019). A mixture of 150 times diluted Aq1 stock solution (25 µl, containing 1 U in total), deionized water (25 µl), sodium carbonate buffer (70 µl; 50 mM; pH 10.0), and substrate solution (70 µl; 1.6 mg N‐succinyl‐ala‐ala‐pro‐phe‐ p ‐nitroanilide in 1.0 ml of the same buffer) was incubated at 50°C for 20 min.…”

Section: Methodsmentioning

confidence: 99%

“…It is hence of interest to impact on gluten during different stages of bread baking. That aqualysin 1 (Aq1) is subject to heat‐sensitive inhibition makes it a potent tool for studying the contribution of gluten to bread loaf volume, crumb structure, and texture (Verbauwhede et al., 2018; Verbauwhede, Lambrecht, Fierens, et al, 2019; Verbauwhede, Lambrecht, Jekle, et al, 2019). In addition, appropriate peptidase use results in soft fresh bread crumb and delays crumb firming and the subsequent increase of its chewiness during storage (Caballero, Gomez, & Rosell, 2007; Indrani, Prabhasankar, & Venkateswara Rao, 2003; Mathewson, 2000).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Heat‐sensitive inhibition of aqualysin 1 by protein containing wheat, maize, and barley extracts

et al. 2020

Self Cite

View full text Add to dashboard Cite

Background and objectives Wheat flour proteins inhibit the thermo‐active serine peptidase aqualysin 1 (Aq1) from Thermus aquaticus in a temperature‐dependent way. The impact of aqueous flour extracts (FEs) from maize, barley, or rice on Aq1 activity both in an assay and in a gluten‐starch model system (GSMS) for bread making was investigated. Findings The degree of Aq1 inhibition by maize and barley FEs decreased at temperatures exceeding 50°C. With higher levels of FEs, higher temperatures were required to undo inhibition. Rice FEs did not inhibit Aq1. Gluten hydrolysis started at lower temperatures in GSMS containing maize FE rather than wheat FE. Incubating Aq1 with maize FE prior to inclusion in GSMS containing wheat FE decreased the onset temperature of Aq1 activity. Conclusions In presence of their FEs, the onset and optimal temperatures for Aq1 activity increased in the order maize, wheat, and barley. When Aq1 was incubated with maize inhibitors prior to dough making, wheat inhibitors still impacted Aq1 activity. Significance and novelty That maize and barley contain inhibitors inactivating Aq1 in a heat‐sensitive way different from that exerted by those in wheat is novel and relevant in the context of the production of multigrain bread products.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Heat‐sensitive inhibition of aqualysin 1 by protein containing wheat, maize, and barley extracts

et al. 2020

Self Cite

View full text Add to dashboard Cite

show abstract

“…Wheat flour (10.0 g; 14.0% moisture), 2.0 ml 0.032% (w/v) rhodamine B and deionized water (3.9 ml) that did or did not contain Aq1 [150 ± 5 U/g flour protein as in Verbauwhede et al (2018) and Verbauwhede et al (2019) or 1,200 ± 5 U/g flour protein] were mixed for 180 s with a 10 g pin mixer (National Manufacturing, Lincoln, NE, USA).…”

Section: Dough Makingmentioning

confidence: 99%

“…On molecular scale, Aq1 use increases the extractability of protein from bread crumb in sodium dodecyl sulfate (SDS) and salt containing media through release of peptides from the repetitive gluten domains (Verbauwhede et al, 2018;Verbauwhede et al, 2019). As a result, the thermoset gluten network in these breads mainly consists of peptides from non-repetitive protein domains (Verbauwhede et al, 2019). On macroscale, Aq1 use affects neither bread loaf volume nor its crumb structure (Verbauwhede et al, 2018).…”

Section: Introductionmentioning

confidence: 99%

Microscopic investigation of the formation of a thermoset wheat gluten network in a model system relevant for bread making

Verbauwhede

Lambrecht

Jekle

et al. 2019

Int J of Food Sci Tech

Self Cite

View full text Add to dashboard Cite

Although the impact of heat on molecular properties of wheat gluten is well understood, changes in its microstructure have rarely been studied. Here, formation of the thermoset gluten network in a model system relevant for bread baking was studied with confocal laser scanning microscopy and protein network analysis. From 65 °C onwards, gluten converts from thick aligned protein strands in a highly branched and homogeneous network of small thin protein threads. Neither gliadin incorporation in the network nor application of aqualysin 1, the thermo-active serine peptidase from Thermus aquaticus which recently has been reported to hydrolyze gluten proteins in dough only at temperatures exceeding 80 °C, impacts on the gluten microstructure. As starch causes structure setting itself and thereby decreases protein mobility, molecular scale changes in the gluten network at temperatures exceeding 80 °C brought about by aqualysin 1 do not impact its microstructure.

show abstract

The effect of continuous cooking on the properties of spaghetti and its cooking water

Diamante¹,

Deleu

Turrin

et al. 2022

Cereal Chem

Self Cite

View full text Add to dashboard Cite

Background and Objectives In catering environments, subsequent batches of pasta are cooked in the same water to save water and energy. This results in formation of a foam layer made up by solids leached from the pasta. Here, the effect of cooking up to 13 subsequent batches on spaghetti cooking and foaming of the cooking water was investigated. Cooking at acidic pH was also studied for a single batch. Findings Water uptake by dry spaghetti decreases with batch number. The increasingly lower mobility in the network of swollen starch and polymerized protein network reduces the extent to which albumins and globulins are leached out. Evidently, the solid content in the cooking water increases with batch number while its pH drops. Separation of pasta fragments from the cooking water does not significantly affect (p > 0.05) the foam stability. Significance and Novelty This study provides additional insights in the composition and foaming properties during the continuous cooking process of pasta.

show abstract

Impact of aqualysin 1 peptidase from Thermus aquaticus on molecular scale changes in the wheat gluten network during bread baking

Cited by 7 publications

References 24 publications

Heat‐sensitive inhibition of aqualysin 1 by protein containing wheat, maize, and barley extracts

Heat‐sensitive inhibition of aqualysin 1 by protein containing wheat, maize, and barley extracts

Microscopic investigation of the formation of a thermoset wheat gluten network in a model system relevant for bread making

The effect of continuous cooking on the properties of spaghetti and its cooking water

Contact Info

Product

Resources

About