Transglutaminase Protein Substrates of Food Interest

Giosafatto, C. Valeria L.; Al-Asmar, Asmaa; Mariniello, Loredana

doi:10.1007/978-981-13-1933-4_15

Cited by 12 publications

(12 citation statements)

References 125 publications

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“…Hence, representing a good source of proteins in human diets, they are consumed worldwide [94]. The bean proteins act, as the proteins from different legumes, as mTGase substrate [22,93,94]. In particular, Romano et al [93] investigated the influence of mTGase treatment on several properties of Phaseolus vulgaris flour prepared from both whole and shelled beans.…”

Section: White Bean Proteinsmentioning

confidence: 99%

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Microbial Transglutaminase as a Tool to Improve the Features of Hydrocolloid-Based Bioplastics

Giosafatto

Fusco

Al-Asmar

et al. 2020

IJMS

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Several proteins from animal and plant origin act as microbial transglutaminase substrate, a crosslinking enzyme capable of introducing isopeptide bonds into proteins between the aminoacids glutamines and lysines. This feature has been widely exploited to modify the biological properties of many proteins, such as emulsifying, gelling, viscosity, and foaming. Besides, microbial transglutaminase has been used to prepare bioplastics that, because made of renewable molecules, are able to replace the high polluting plastics of petrochemical origin. In fact, most of the time, it has been shown that the microbial enzyme strengthens the matrix of protein-based bioplastics, thus, influencing the technological characteristics of the derived materials. In this review, an overview of the ability of many proteins to behave as good substrates of the enzyme and their ability to give rise to bioplastics with improved properties is presented. Different applications of this enzyme confirm its important role as an additive to recover high value-added protein containing by-products with a double aim (i) to produce environmentally friendly materials and (ii) to find alternative uses of wastes as renewable, cheap, and non-polluting sources. Both principles are in line with the bio-economy paradigm.

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Section: White Bean Proteinsmentioning

confidence: 99%

“…Figure 2. Intra-(A) and inter-(B) isopeptide bond between glutamine and lysine catalyzed by mTGase (modified from Giosafatto et al[22]). …”

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confidence: 99%

Microbial Transglutaminase as a Tool to Improve the Features of Hydrocolloid-Based Bioplastics

Giosafatto

Fusco

Al-Asmar

et al. 2020

IJMS

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“…2 In contrast to those plant and mammal transglutaminases, the transglutaminase produced by S. mobaraenesis (smTG) is calcium-independent, safe, and cost-effective. 3 Currently, smTG has become the leading commercial transglutaminase product and is widely used to improve protein-based foods' texture. 4 In the past 15 years, the attempts to use S. mobaraenesis transglutaminase for inducing antibody-drug conjugation, 5 PEGylation of proteins, 6 DNA fluorescence labeling, 7 and click chemistry 8 have expanded its application perspective.…”

Section: ■ Introductionmentioning

confidence: 99%

Significantly Improving the Thermostability and Catalytic Efficiency of Streptomyces mobaraenesis Transglutaminase through Combined Rational Design

Wang

Zhao

et al. 2021

J. Agric. Food Chem.

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Streptomyces mobaraenesis transglutaminase has been widely used in food processing. We here significantly improved the catalytic properties of S2P-S23V-Y24N-S199A-K294L (TGm1), a highly stabilized variant of the transglutaminase. First, a virtual proline scan was performed based on folding free energy changes to obtain TGm1 variants with enhanced thermostability. Second, the residues within 15 Å of Cys64 in the enzyme–substrate complex of TGm1 were subjected to virtual saturation mutagenesis to generate the variants with reduced binding free energy and increased activity. After combining the favorable mutations, we obtained the variant FRAPD-TGm1-E28T-A265P-A287P (FRAPD-TGm2), exhibiting 66.9 min of half-life at 60 °C (t 1/2(60 °C)), 67.8 °C of melting temperature (T m), and 71.8 U/mg of specific activity, which are 2-fold, 2.6 °C, and 43.8% higher than those of FRAPD-TGm1, respectively. At last, to increase the surface negative net charge of FRAPD-TGm2, we introduced the mutations N96E-S144E-N163D-R183E-R208E-K325E, yielding FRAPD-TGm3. The latter’s t 1/2(60 °C), T m, and specific activity were 122.9 min, 68.6 °C, and 83.7 U/mg, which are 83.8%, 0.8 °C, and 16.6% higher than the former, respectively. FRAPD-TGm3 is thus a robust candidate for transglutaminase application.

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“…Microbial transglutaminase (TGase) belongs to a family of enzymes (E.C. 2.3.2.13) (widely distributed in nature from microbes to animals and plants) capable of catalyzing iso–peptides bonds between endo-glutamine and endo-lysine residues belonging to proteins of different nature, giving arises to intra- and inter-molecular crosslinks [ 2 , 11 ]. TGase is widely used in the food industry as technological aid.…”

Section: Introductionmentioning

confidence: 99%

Hydrocolloid-Based Coatings with Nanoparticles and Transglutaminase Crosslinker as Innovative Strategy to Produce Healthier Fried Kobbah

Al-Asmar

Giosafatto

Sabbah

et al. 2020

Foods

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This study addresses the effect of coating solutions on fried kobbah. Coating solutions were made of pectin (PEC) and grass pea flour (GPF), treated or not with transglutaminase (TGase) and nanoparticles (NPs)—namely mesoporous silica NPs (MSN) or chitosan NPs (CH–NPs). Acrylamide content (ACR), water, oil content and color of uncoated (control) and coated kobbah were investigated. Zeta potential, Z-average and in vitro digestion experiments were carried out. Zeta potential of CH–NPs was stable from pH 2.0 to pH 6.0 around + 35 mV but decreasing at pH > 6.0. However, the Z-average of CH–NPs increased by increasing the pH. All coating solutions were prepared at pH 6.0. ACR of the coated kobbah with TGase-treated GPF in the presence nanoparticles (MSN or CH–NPs) was reduced by 41.0% and 47.5%, respectively. However, the PEC containing CH–NPs showed the higher reduction of the ACR by 78.0%. Water content was higher in kobbah coated by PEC + CH–NPs solutions, while the oil content was lower. The color analysis indicated that kobbah with lower browning index containing lower ACR. Finally, in vitro digestion studies of both coating solutions and coated kobbah, demonstrated that the coating solutions and kobbah made by means of TGase or nanoparticles were efficiently digested.

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Transglutaminase Protein Substrates of Food Interest

Cited by 12 publications

References 125 publications

Microbial Transglutaminase as a Tool to Improve the Features of Hydrocolloid-Based Bioplastics

Microbial Transglutaminase as a Tool to Improve the Features of Hydrocolloid-Based Bioplastics

Significantly Improving the Thermostability and Catalytic Efficiency of Streptomyces mobaraenesis Transglutaminase through Combined Rational Design

Hydrocolloid-Based Coatings with Nanoparticles and Transglutaminase Crosslinker as Innovative Strategy to Produce Healthier Fried Kobbah

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