2011
DOI: 10.1094/cchem-07-11-0082
|View full text |Cite
|
Sign up to set email alerts
|

Rheology, Microstructure, and Baking Characteristics of Frozen Dough Containing Rhizopus chinensis Lipase and Transglutaminase

Abstract: The beneficial effects of a new recombinant lipase (Rhizopus chinensis lipase [RCL]) and transglutaminase (TG) were investigated on frozen dough systems and their breadmaking quality. Rheological properties and microstructure of doughs were measured using a dynamic rheometer, rheofermentometer F3, and scanning electron microscopy (SEM). Measurements of viscoelastic properties showed that both G′ and G″ of dough containing RCL and TG were greater than those of the control after 35 days of frozen storage. The SE… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

3
29
0

Year Published

2014
2014
2021
2021

Publication Types

Select...
5
1

Relationship

2
4

Authors

Journals

citations
Cited by 36 publications
(32 citation statements)
references
References 26 publications
3
29
0
Order By: Relevance
“…In an earlier study (Huang, Yuan, Kim, & Chung, 2008), the use of transglutaminase improved frozen dough quality through its protein polymerization ability which stabilized the gluten structure embedded in the starch granules. Similar synergistic findings were reported in doughs containing recombinant lipase (Rhizopus chinensis lipase) and transglutaminase enzymes stored at −18°C for 7-35 days; rheofermentative and water holding capacities of the frozen dough were improved (Li et al, 2011). In another study , transglutaminase treatment significantly decreased the ratio of HMW-GS: LMW-GS and GMP content in fresh dough and GMP particle size increased.…”
Section: Enzymessupporting
confidence: 75%
See 1 more Smart Citation
“…In an earlier study (Huang, Yuan, Kim, & Chung, 2008), the use of transglutaminase improved frozen dough quality through its protein polymerization ability which stabilized the gluten structure embedded in the starch granules. Similar synergistic findings were reported in doughs containing recombinant lipase (Rhizopus chinensis lipase) and transglutaminase enzymes stored at −18°C for 7-35 days; rheofermentative and water holding capacities of the frozen dough were improved (Li et al, 2011). In another study , transglutaminase treatment significantly decreased the ratio of HMW-GS: LMW-GS and GMP content in fresh dough and GMP particle size increased.…”
Section: Enzymessupporting
confidence: 75%
“…This notion was confirmed in a study by Steffolani, Ribotta, Perez, Puppo, and León (2012), where transglutaminase added at intermediate levels resulted in the largest bread volume compared to control (without added enzymes) and other two enzyme (pentosanase and glucose oxidase) samples of frozen dough stored at −18°C for 0-9 weeks. Additionally, the samples had a more open network and uniform crumbs, higher specific volume with higher sensory scores for the product (Li et al, 2011). However, lipase known to catalyze hydrolysis and/or synthesize the ester bond (s) of glycerol (phospho-or glycol) lipids (Gerits, Pareyt, Decamps, & Delcour, 2014) had no effect on GMP particle size , but its specificity to lipid fractions in frozen dough may exert major roles in gas incorporation and stabilization after frozen storage (Pareyt, Finnie, Putseys, & Delcour, 2011).…”
Section: Enzymesmentioning
confidence: 99%
“…Among other reasons, the loss of GMP after TG treatment has been attributed to an increased SDS solubility owing to structure changing of glutenins (Steffolani et al 2008). TG catalyzes the formation of isopeptide bonds producing large protein polymers, which increase the water-holding capacity of dough and reduce its freezable water content (Li et al 2011). The GMP content decreased as the frozen storage time increased (Table I).…”
Section: Resultsmentioning
confidence: 99%
“…Changes in free thiol groups were determined according to the method of Li et al (2011) using Ellman's reagent, which contained 4 mg of 5,59-dithiobis-2-nitrobenzoic acid in 1 mL of Tris-glycine buffer (pH 8.0) and was prepared daily. First, 0.2 g of dough (fresh or thawed) was suspended in 1 mL of guanidine hydrochloride (GuHCl)/Tris-glycine solution, which consisted of Tris-glycine buffer (8.5mM Tris, 9.2mM glycine, and 0.3mM ethylenediaminetetraacetic acid, pH 8.0) and 5M GuHCl.…”
Section: Methodsmentioning
confidence: 99%
See 1 more Smart Citation