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This study investigated the potential of fortifying a probiotic yogurt with cantaloupe rind powder. The raw cantaloupe rind powder was subjected to enzyme treatment to enhance its soluble fiber content. The effects of incorporating raw and enzyme-treated cantaloupe rind powder (referred as RCRP and ECRP, respectively) on the physicochemical properties, textural and rheological properties, antioxidant properties and syneresis of yogurt were evaluated during a 15-day storage period at 4 °C. The results revealed that the inclusion of RCRP resulted in a reduction in yogurt hardness, viscosity, elasticity and stability compared to the control yogurt without cantaloupe rind powder fortification. In contrast, adding ECRP led to an increase in the hardness, viscosity, elasticity and stability of the yogurt. Specifically, on day 15 of storage, the syneresis of ECRP-fortified yogurt was approximately 3 times lower, while that value of RCRP-fortified yogurt was approximately 2 times higher compared to the control yogurt. Notably, the RCRP- and ECRP-fortified yogurts displayed 14- and 9-times higher antioxidant activity, respectively, compared to the control yogurt. This study suggests that employing enzyme treatment on cantaloupe rind powder holds promise as an approach to yield positive effects when incorporating the powder into yogurt, particularly in terms of stability, textural and rheological properties. • Enzyme treatment increased the soluble dietary fiber content of cantaloupe rind powder. • Raw powder had negative but enzyme-treated powder had positive impacts on yogurt stability, texutre and rheology. • Both types of powder improved antioxidant properties of yogurt. • Enzyme treatment offers a promising method to boost soluble fiber in food by-products for beneficial yogurt incorporation. [ABSTRACT FROM AUTHOR]

Acrylamide is the main contaminant for starchy foods cooked at temperatures above 120 °C. It represents a potential carcinogen, and consequently, its reduction is important for safeguarding global health. The L-asparaginase enzyme catalyses the hydrolytic cleavage of L-asparagine, a precursor of acrylamide, into L-aspartic acid and ammonia, thus reducing the formation of acrylamide. The objective of this work was to test the enzyme L-asparaginase at two concentrations (150 and 300 U/kg flour) under normal baking conditions to reduce acrylamide. The results showed that the use of 300 U/g of the enzyme led to a reduction of 78% in acrylamide, meeting the reference level reported by Reg. (EU) 2017/2158 (50 μg/kg) without influencing parameters such as colour that impact the final characteristics of the product. • The effect of treatment with L-asparaginase for acrylamide mitigation in homemade bread was studied. • Two concentrations (150 U/Kg of flour e 300 U/Kg of flour) of L-asparaginase were tested. • L-asparaginase was capable of reducing 78% of acrylamide in homemade bread. [ABSTRACT FROM AUTHOR]

Blueberry ( Vaccinium corymbosum L.) fruit, rich in anthocyanins, polyphenolics and antioxidant activity, has not been exploited fully for processing into juice. The objective of this study was to investigate the effect of commercial juice extraction enzymes (Cellubrix, Pectinex Ultra SPL, and Crystalzyme) on juice yield, total soluble solids (TSS), juice clarity, HPLC sugars profile, total anthocyanins (ACY), total phenolics (TPH), and antioxidant activity (assayed as FRAP). Enzyme treatments resulted in significantly ( p ≤ 0.05) higher juice yield (86.91–87.29 mL/100 g with Pectinex and Crystalzyme as compared to 79.45 mL/100 g from control), higher juice clarity, and titratable acidity, and lower extraction loss. However, enzymes treatment had no effect on total soluble solids (°Brix), fructose, glucose, and total sugars. Generally, juice Hunter color values (L, a, and b), Hue angle (h°) and Chroma (C*) were affected positively by the enzymes treatment. As compared to the control (9.69 mg/100 mL), total ACY were significantly higher (11.49–12.90 mg/100 mL) in juice from enzyme-treated macerates; whereas there was no effect on TPH, determined as gallic acid equivalent (96-89‒101.30 mg GAE/100 mL) and FRAP antioxidant activity (3.87–3.97 μmol TE/100 mL). Total ACY, TPH, and FRAP were several-fold higher in the pomace than the juice. [ABSTRACT FROM AUTHOR]

Abstract: The aim of work was optimization of technology of cloudy blackcurrant and plum juices production. The major concern was the increase of product cloudiness and its stability. Red fruit were processed with commercial pectinolytic preparations (Pectinex BE Colour, Pectinex BE XXL, and mixture of Rohapect PTE with Rohament PL). The effect of enzyme dose, maceration time and addition of ascorbic acid (in case of plum) on juices quality was investigated. Using single enzyme, either polygalacturonase or pectin lyase did not allow obtaining juices with high enough turbidity, however appropriate enzyme mixture allowed to obtain cloudy juice with the turbidity of at least 230 NTU for blackcurrant and above 500 NTU for plum juice. The best pressing-yield for blackcurrant was achieved with polygalacturonase and pectin lyase, 65 g/100 g after 1 h and 74 g/100 g after 4 h of pectinolysis. The macerating mixture gave about 58÷59 g/100 g yield, irrespectively of enzymation time. Pressing-yield of plum juices was in the range of 94÷97 g/100 g due to the fact that practically only skins were retained on pressing cloth. Addition of ascorbic acid (AA) during plum juice processing in quantity of 500 mg/kg had protective effect on anthocyanins. In control plum juices range of anthocyanins contents were 12.1÷16.5 mg/100 ml while in juice with AA addition even 21.4÷24.5 mg/100 ml. [Copyright &y& Elsevier]

There is a growing consumption on puffer fish-based food since this species contains high nutritional properties in terms of high protein and low fat values. However, this is hampered by the tough texture of puffer muscle. In this study, a simple but robust strategy to improve the tenderness of puffer muscle by papain treatment of different concentration (60, 80, 100, 120 and 140 U/mL) was developed. Results showed that the shear force and the hardness of fish muscle decreased significantly with increasing papain concentration, indicating improved tenderness of fish muscle. Protein patterns from SDS-PAGE confirmed that the papain-treated muslces had increasing degrees of degradation with faded myosin heavy chain (MHC) band and actin band as well as an increasing amount of low molecular weight pepeptides around 25–35 kDa. This may associated with the loss of one major protein denaturation peak as revealed by differential scanning calorimetry (DSC). Conformational characterization showed that the relative content of α -helix decreased, while irregular coil structure increased with increasing papain concentration. These results suggested puffer myofibril proteins, mainly myosin and actin were hydrolyzed into low molecular peptides with more disorder structures, which might be responsible for the improved tenderness. • Papain treatment resulted in improved tenderness of puffer fish muscle. • Degradation of myosin heavy chain and actin was observed after treatment. • Papain treatment led to increase in irregular coil structure but increase in α-helix. • The relation between tenderization and myofibril protein changes was confirmed. [ABSTRACT FROM AUTHOR]

To understand the interactions between enzyme-modified potato proteins and potato starch, herein transglutaminase or peroxidase was used to create covalent crosslinked structure of potato protein. The mixtures of native or enzyme-treated protein and potato starch in different proportions were prepared and the structural and physicochemical characteristics were studied. The results revealed that the new covalent and/or noncovalent linkages formed after enzyme modification of potato protein. Compared with the mixtures of native protein and starch, the mixtures of enzyme-treated protein and starch had larger shear resistance (breakdown value decreased by about 2–100 times) and higher gel strength (G′ and G″), but smaller thermal stability (312.3–307.3, 309.1 °C) and lower peak viscosity (decreased by 1.5–4 times). In conclusion, transglutaminase or peroxidase accelerated the formation of cross-networked structure in potato protein, which increased the interaction with starch, hence greatly improving the gel properties of the mixture of protein and starch. • Potato protein was modified with transglutaminase or peroxidase. • Enzymatic modifications resulted in the covalent crosslinked structure of protein. • Enzyme-treated protein/starch had lower thermostability and viscosity, but higher gel strength. [ABSTRACT FROM AUTHOR]

Potato protein (PP) was modified with laccase or tyrosinase to obtain covalent cross-linking structures, and then the blends of native/enzyme-treated protein and potato starch (PS) with different ratios were prepared. The FT-IR results suggested the interactions between protein and starch strengthened after enzyme treatment. The relative crystalline raised to 26–29% after the protein mixing with starch. The thermal degradation temperatures of the blends of enzyme-treated protein and PS (296.71–312.91 °C) were apparently lower than that of the blends of PP:PS (312.31–312.76 °C). Compared to the blends of PP:PS, the peak viscosity, trough viscosity and final viscosity of the blends of enzyme-treated protein and PS decreased by 12.7–41.1%. The blends of enzyme-treated protein and PS had a lower storage modulus than native blends. The outcome would provide a view on the theoretical basis of interactions between protein and starch in exploring favorable potato staple foods. •Covalent cross-linking structure in potato protein was formed by enzyme treatment. •The native/enzyme-treated protein was blended with potato starch with different ratios. •The blends of enzyme-treated protein and starch had lower thermostability. •The blends of enzyme-treated protein and starch had lower paste viscosity. •The blends of enzyme-treated protein and starch had lower storage and loss moduli. [ABSTRACT FROM AUTHOR]