L-theanine is a characteristic non-proteinogenic amino acid found in tea leaves and has attracted considerable attention because of its diverse physiological activity and broad application prospects. γ-glutamyl transpeptidase (GGT) can catalyze the synthesis of L-theanine from L-glutamine and ethylamine without ATP consumption, highlighting its advantages for enzymatic production. In this study, a complete process was established for L-theanine production. Through screening of single and dual promoters, the optimal expression combination, PyxiE-PspoVG, was identified. Furthermore, by integrating the dal selection marker, an antibiotic-free engineered strain was developed. After flask-level optimization, the GGT activity reached 27.32 U/mL and further increased to 127.37 U/mL in 3 L fed-batch fermentation. Using the fermentation broth as the biocatalyst, fed-batch conversion of 0.6 M L-glutamine and 2 M ethylamine yielded 0.52 M (91.44 g/L) L-theanine within 24 h. Further integration of ceramic membrane filtration, ultrafiltration, nanofiltration, electrodialysis, activated-carbon decolorization and ethanol crystallization afforded a final product purity of 95.6%. This study offers a useful reference for large-scale L-theanine production.

L-Theanine (L-Th), is synthesized through gamma-glutamyltransferase (GGT; EC 2.3.2.2) using L-glutamine and ethylamine. To boost productivity, we applied semi-rational mutagenesis to the Bacillus amyloliquefaciens SK11.001 GGT and obtained 16 variants. The mutant enzymes T398P and I267L exhibited higher transpeptidase activities (16.33 U center dot mL-1 and 14.09 U center dot mL-1) and increased transpeptidase/hydrolase activity (2.5-fold and 1.8-fold). Under optimal conditions, the yield of L-Th reached 191.9 mM (T398P) and 185.7 mM (I267L). Threedimensional modeling analysis revealed that the donor substrate L-glutamine forms a new hydrogen bond with S467 within the binding pocket, which stabilizes the ligand and enhances catalytic efficiency. These results suggest that T398P has great potential for L-Th production.

BACKGROUND:Plant proteins, especially legume proteins, have garnered widespread attention due to their rich nutritional value and numerous health benefits. In this study, the flavor properties of soy, pea, mung bean, chickpea, faba bean, and peanut proteins were analyzed and compared using rapid gas chromatography electronic nose (GC-E-Nose), headspace solid-phase microextraction-gas chromatography-mass spectrometry (HS-SPME-GC-MS), and headspace gas chromatography-ion mobility spectrometry (HS-GC-IMS) coupled with chemometrics. RESULTS:GC-E-Nose analysis showed a distinct difference in the volatile compounds of six legume proteins. A total of 208 and 101 volatile compounds were identified using GC-MS and GC-IMS, respectively, with aldehydes, alcohols, and ketones being the main volatile components. Among the six legume proteins, chickpea protein possessed the highest content of volatile compounds, whereas peanut protein contained the largest number of volatile compounds. In the meanwhile, 40 and 33 compounds with variable importance in the projection (VIP) greater than 1 were screened using orthogonal partial least squares discriminant analysis (OPLS-DA), of which 15 (hexanal, nonanal, 2,6-dimethylpyrazine, heptan-2-one, 2,5-dimethylpyrazine, pentan-1-ol, tridecane, tetradecane, oct-3-en-2-one, 1,4-xylene, hexanoic acid, dodecane, 2-pentylfuran, hexan-1-ol, pentanal), and 3 (propan-2-ol, heptan-2-one-D, pentan-1-ol-D) compounds with VIP > 2, respectively. These volatiles were the key differential compounds that distinguished the six legume proteins. GC-MS combined with odor activity value (OAV) identified 35 flavor compounds as key odor active compounds with OAV > 1. CONCLUSION:The combined application of these techniques better characterized the flavor profile differences among legume proteins, providing theoretical guidance for developing new plant-based alternative protein products. © 2025 Society of Chemical Industry.

D-allulose, a low-calorie functional sweetener, is produced by the enzymatic conversion of D-fructose via Dallulose 3-epimerase (DAE) and holds significant market potential, particularly for individuals with obesity and diabetes. However, the limited reusability and stability of DAE have restricted its industrial application. In this study, we developed functional superparamagnetic supports by integrating diatomite, a biomineralized silica- based material, with cobalt ferrite nanoparticles through a green chemical co-precipitation method. The covalent attachment of DAE enzymes to these magnetic supports resulted in enzyme-metal hybrid catalysts (DAE@mDE-NH2) that exhibited enhanced stability and facilitated recovery and reuse via magnetic separation. These catalysts showed superior stability in acidic conditions and high temperatures, with a 24-fold increase in half-life at 60 degrees C compared to free DAE. They also exhibited remarkable durability, retaining 95.36 % of their activity after six months of storage at 4 degrees C and 70.08 % activity after 12 consecutive cycles. Utilizing this robust and recyclable biocatalyst, 147.7 g/L of D-allulose was obtained from 500 g/L of D-fructose. This study presents a sustainable strategy for advancing the production of high-value functional sweeteners like D-allulose while providing new insights into enzyme immobilization for biocatalytic processes.

Maltodextrin is a widely used commodity in the global food industry; however, its applications are limited by physicochemical instability caused by varying degrees of polymerization and high reducing properties. In this study, an enzymatic cascade was developed to synthesize non-reducing maltodextrin with a single degree of polymerization (N-G7) using β-cyclodextrin (β-CD) as the substrate. Cyclodextrinase (CDase) hydrolyzed β-CD into linear oligosaccharides, followed by maltooligosyltrehalose synthase (MTSase)-catalyzed transglycosylation forming a terminal α-1,1-glycosidic bond, imparting non-reducing properties. The enzymatic synthesis of N-G7 was optimized through kinetic analysis, demonstrating that controlled enzyme loading and reaction durations improved yield by balancing CDase-mediated β-CD hydrolysis and MTSase-driven transglycosylation. Notably, fermentation enzyme activities of 38.31 U/mL for CDase and 475.44 U/mL for MTSase were achieved through separate fed-batch fermentations. The synergistic interaction between these enzymes was governed by Le Chatelier’s principle, where MTSase-mediated transglycosylation drove the equilibrium shift from β-CD hydrolysis (catalyzed by CDase) to N-G7 synthesis, ultimately achieving a 57.3

D-allulose, a functional rare sugar produced by D-allulose 3-epimerase (DAE), is recognized for its benefits in weight management and diabetes care. However, the poor stability and reusability of free DAE hinder its continuous industrial production. Continuous flow bioreactors are ideal for sustainable production, yet research on continuous D-allulose synthesis remains scarce. In this work, we developed immobilized DAE enzymes on lowcost modified diatomite for use in packed-bed reactors (PBR) for continuous D-allulose synthesis, investigating two immobilization strategies: a two-step method and a one-step direct cross-linking method. The resulting immobilized enzymes showed 12 to 16 times higher thermal stability than free DAE and retained good storage stability. In continuous-flow reactions, these biocatalysts demonstrated outstanding operational stability, consistently maintaining product yields above 20% over 30 days. Additionally, we designed a dual-enzyme cascade within the PBR, achieving one-step conversion of glucose to D-allulose with a 15% conversion rate and 76% yield retention after six cycles. When applied to fruit and vegetable waste, the cascade system produced 11-18 g of D-allulose per kg of fruit residues and 9-11 g per kg of vegetable residues. This study provides a scalable, cost-efficient solution for continuous D-allulose production, with significant potential for sustainable food ingredient manufacturing and waste valorization.

Thymol, a bioactive compound, offers significant potential in functional foods but its application is limited by poor stability, solubility and bioavailability. This study aimed to enhance thymol's stability and bioactivity by encapsulating it in pullulan-whey protein isolate-based electrospun nanofibers and evaluating its effects in bread fortification. The impact of encapsulation on thymol's recovery, functional properties, bioavailability and cytotoxicity was assessed. The results showed that bread fortified with thymol encapsulated pullulan-whey protein isolates-based nanofiber (THY-PW-NF) significantly improved flour pasting properties and bread texture, while also enhancing thymol's recovery (78.07 %) during bread preparation compared to using free thymol. THY-PW-NF in bread preserved its bioactivity after gastrointestinal digestion. It increased its inhibitory effects on alpha-amylase, alpha-glucosidase and pancreatic lipase as revealed by molecular docking and molecular dynamic simulations. Cytotoxicity assays on Caco-2 cells confirmed that exposure to free thymol, thymol extracted from nanofibers and THY-PW-NF derived from fortified bread within a concentration range of 0-20 μg/mL did not significantly impact cell viability compared to control cells over 24 h. These findings suggest that encapsulation effectively incorporates thymol into functional foods, maintaining its health benefits without compromising safety.

This study aims to enhance the oxidative stability of fish oil through encapsulation in pullulan/sodium caseinate (PUL/NaCAS) nanofibers. Electrospinning was employed to produce three formulations: control (0% fish oil) and samples with 5% and 10% fish oil. Characterization of the emulsions showed that increasing oil content led to larger droplet size and reduced viscosity. Scanning electron microscopy (SEM) analysis revealed surface imperfections and a gradual increase in fiber diameter with higher oil loading. Fourier transform infrared (FTIR) spectroscopy confirmed molecular interactions, and fibers with 10% fish oil showed a shift toward a more amorphous structure. Fish oil incorporation also enhanced hydrophobicity and thermal stability, as indicated by thermal and wettability measurements. Antioxidant assays include 2,2-diphenyl-1-picrylhydrazyl (DPPH), 2,2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), and total phenolic content (TPC), which showed the highest bioactivity at 5% fish oil, with a slight decrease at 10%, likely due to structural saturation. Encapsulation at 5% fish oil significantly reduced lipid oxidation during storage (hydroperoxide values decreased from 8.6 to 4.8 mM at 60 °C/15 days), demonstrating the protective effect of the nanofiber matrix. Docking and density functional theory (DFT) analyses confirmed stable DHA/EPA–caseinate interactions and increased electronic stability, supporting the experimental results. Compared with conventional carriers such as spray-dried or maltodextrin-based systems, PUL/NaCAS nanofibers offered superior oxidative stability, bioactivity, and a biodegradable matrix. Overall, the 80PUL:20NaCAS:5% fish oil formulation represents a versatile platform for stabilizing omega-3 oils, with potential applications in food preservation, nutraceutical delivery, and functional packaging.

D-allulose, a low-calorie rare sugar, can be biosynthesized by D-allulose 3-epimerase (DAE). Here, DAE was covalently immobilized on polyethyleneimine-modified diatomite using two methods: a biopolymer coating approach (DAE@PEI-GA@PDP) and a direct attachment method (DAE-GA@PEI@PDP). Both immobilized DAE enzymes exhibited enhanced thermal stability and broader pH tolerance compared to the free DAE. They also exhibited excellent reusability and maintained more than 70% of their activity after 10 cycles. Additionally, a multienzyme cascade system was developed to produce D-allulose from low-cost D-glucose using immobilized glucose isomerase (GI) and immobilized DAE enzymes. This system obtained 76 g/L D-allulose from 500 g/L Dglucose. Notably, the application was extended to fruit tea drinks, successfully transforming high-calorie sugars (D-glucose and D-fructose) into D-allulose. This research offers a promising immobilization strategy for DAE on silica-based materials and provides robust biocatalysts for creating functional fruit tea drinks aimed at diabetics and individuals with specific dietary needs.

Limited and unclear research exists on the individual capacity of major fractions of pea protein legumin (PL), vicilin (PV) and albumin (PA), which collectively contribute to the structural and functional properties of pea protein. Findings revealed that PV (72.26 ± 2.6 %) and PA (57.42 ± 4.1 %) displayed better solubility compared to PL. PL fraction possessed a complex three-dimensional structure, higher surface hydrophobicity (So), and superior oil-holding-capacity (OHC) contributing to its 4-fold strength (8.58 ± 0.5 N) and structured gel formation. The smaller particle size of PA was also accountable for the comparatively weaker gels and unstable emulsions compared to PL, while PV had the least emulsifying capacity, by non-uniform droplet distribution in CLSM served as proof. PL was found to be responsible for gelation, emulsification, and foaming in pea protein due to structural factors (relative abundance of α-helix and β-sheet). While, the flexible structure of PV, absence of cysteine residues, and disulfide bridges played a role in characteristics like foaming stability. Some protein in PV gel was found loose and did not appear to participate in gelation, hence forming a significantly weaker gel than PL. Despite relatively less So and complex structure, albumin (PA) had a smoother but weaker gel, more consistent and a smaller droplet size distribution in emulsions (compared to PV). Nonetheless, this study aims to fill a forgotten gap by providing baseline knowledge on the individual fractions of pea protein, defining their roles and paving the path for future research focusing on structural and functional properties of pea protein.

D-allulose, an ideal low-calorie sweetener, is primarily produced through the isomerization of D -fructose using Dallulose 3-epimerase (DAE; EC 5.1.3.30). Addressing the gap in available immobilized DAE enzymes for scalable commercial D-allulose production, three core-shell structured organic-inorganic composite silica-based carriers were designed for efficient covalent immobilization of DAE. Natural inorganic diatomite was used as the core, while 3-aminopropyltriethoxysilane (APTES), polyethyleneimine (PEI), and chitosan organic layers were coated as the shells, respectively. These tailored carriers successfully formed robust covalent bonds with DAE enzyme conjugates, cross-linked via glutaraldehyde, and demonstrated enzyme activities of 372 U/g, 1198 U/g, and 381 U/g, respectively. These immobilized enzymes exhibited an expanded pH tolerance and improved thermal stability compared to free DAE. Particularly, the modified diatomite with PEI exhibited a higher density of binding sites than the other carriers and the PEI-coated immobilized DAE enzyme retained 70.4 % of its relative enzyme activity after ten cycles of reuse. This study provides a promising method for DAE immobilization, underscoring the potential of using biosilica-based organic-inorganic composite carriers for the development of robust enzyme systems, thereby advancing the production of value-added food ingredients like D-allulose.

Inherently chiral medium-ring derivatives have important applications in many research fields, such as materials science, molecular recognition, and asymmetric catalysis. However, the enantioselective assembly of these molecules, especially by organocatalytic strategies, remains a formidable challenge, and few methods are available. Here, we report the enantioselective NHC-catalyzed (NHC: N-heterocyclic carbenes) formal high-order (5 + 3) annulation of 1-(2-indolyl)naphthalen-2-ols with ynals. In the presence of an NHC pre-catalyst, base, Lewis acid and oxidant, this protocol enables the catalytic formation of C-C and C-O bonds, providing practical and facile access to an array of inherently chiral saddle-shaped eight-membered lactones featuring an oxocin-2-one scaffold with structural diversity in good efficiency and excellent enantiocontrol. Moreover, the scale-up preparation and representative late-stage transformations of the eight-membered lactones further demonstrate the application potential of this synthetic technology. Inherently chiral medium-ring derivatives have important applications in many research fields, but few enantioselective methods are available. Herein, the authors report the enantioselective N-heterocyclic carbenes-catalyzed formal (5 + 3) annulation of 1-(2-indolyl)naphthalen-2-ols with ynals for the synthesis of eight-membered lactones.

Pea protein-based diets have garnered global attention as a viable alternative to meat or primary protein sources. Nevertheless, the utilization of pea protein is hindered by issues such as solubility, and emulsifying properties. This research presents a combined set of techniques employed to commercially available Pea Protein Isolate (PPI) to effectively address major setbacks associated with the usage of pea protein in diverse industrial sectors, especially meat. The set integrates pH at 10.0, sonication at three different magnitudes (1,2 and 4 W/mL), heat at 60°C, and enzyme hydrolysis through Flavourzyme at three different enzyme-to-substrate ratios (0.25%, 0.5%, and 1.0%). Among the twelve treatments, PPI11, PPI12, and PPI13 showed promising outcomes for artificial meat. The treatments exhibited favorable solubility, gelling, emulsifying, and foaming properties while containing the optimum and desirable protein size after undergoing partial hydrolysis comprehended in the gel electrophoresis results. Solubility (for PPI11, PPI12, PPI13) had seen significant (p < 0.05) improvement from 31.03% ± 2.11% (Control) to 64.43% ± 2.09%, 66.23% ± 2.11%, and 69.87% ± 1.57%, accompanied by changes in protein morphology in scanning electron microscopy. Furthermore, treated PPIs were applied to stabilize sunflower oil-in-water emulsion, showing a significant escalation in emulsion capacity (38.46%, 39.42% and 66.61% increase for PPI11, PPI12, PPI13), foaming capacity (46.88%, 51.20%, and 69.60% increase for PPI11, PPI12, PPI13), and foaming stability (30 min) (23.97%, 28.70%, and 30.22% increase for PPI11, PPI12, PPI13). Gelling properties were decisive in this study (2.512 ± 0.1 N, 2.604 ± 0.1 N, and 2.168 ± 0.3 N, for PPI11, PPI12, and PPI13), predominantly in plant-based meat analog perspective. So the mechanism proposed through this research will enable pea protein treated with this set of operations, combining physical, chemical and enzymatic treatments, to further its journey towards considerably improved meat analogs.

Alginate lyases (ALys) whose degrading products, alginate oligosaccharides, exhibit various outstanding biochemical activities have aroused increasing interest of researchers in the marine bioresource field. However, their predominant sourcing from marine bacteria, with limited yields and unclear genetic backgrounds, presents a challenge for industrial production. In this study, ALys (Aly01) from Vibrio natriegens SK 42.001 was expressed in Bacillus subtilis (B. subtilis), a nonpathogenic microorganism recognized as generally safe (GRAS). This accomplishment was realized through a comprehensive strategy involving vector and host selection, promoter and signal peptide screening, and engineering of the ribosome binding site (RBS) and the N-terminal coding sequence (NCS). The optimal combination was identified as the pP43NMK and B. subtilis WB600. Among the 19 reported strong promoters, PnprE exhibited the best performance, showing intracellular enzyme activities of 4.47 U/mL. Despite expectations, dual promoter construction did not yield a significant increase. Further, SPydhT demonstrated the highest extracellular activity (1.33 U/mL), which was further improved by RBS/NCS engineering, reaching 4.58 U/mL. Finally, after fed-batch fermentation, the extracellular activity reached 18.01 U/mL, which was the highest of ALys with a high molecular weight expressed in B. subtilis. These findings are expected to offer valuable insights into the heterologous expression of ALys in B. subtilis.

The encapsulation of thymol blends was examined for two distinct food polymers, pullulan and whey protein isolate at a concentration of 80:20 (PUL:WPI w/w) through coaxial electrospinning. Scanning electron microscopy (SEM) presented clear illustrations of successful thymol encapsulation in nanofibers with bead -like structures and increased diameter as compared to nanofibers without thymol. The maximum encapsulation efficiency (87.05 +/- 1.18%) and loading capacity (17.41 +/- 0.24%) of thymol (2%) in (80:20) PUL:WPI nanofibers (THY -WP -NF) have been achieved. The attenuated total reflectance -Fourier transform infrared spectroscopy (ATR-FTIR) peaks indicated the presence of thymol within the nanofibers, while X-ray diffraction results demonstrated that the thymol existed in an amorphous state within the nanofibers. Furthermore, the encapsulation process led to an increase in the stability (under light and temperature) of thymol, as well as facilitated targeted release in the small intestine. THY-PW-NF exhibited better in -vitro inhibition activity against alphaamylase (66.44%), alpha-glucosidase (80.37%) and pancreatic lipase enzymes (65.60%), along with DPPH and ABTS radicals. Conclusively, THY-PW-NF can be utilized in food and pharmaceutical products owing to a large surface area with improved water solubility, antioxidant activity, high -temperature stability and antidiabetic activity of thymol.

BACKGROUNDFructo-oligosaccharide (FOS) belongs to the group of short inulin-type fructans and is one of the most important non-digestible bifid-oligosaccharides capable of biotransforming sucrose using fructosyltransferase (FTase). However, there are no immobilized FTase products that can be successfully used industrially. In this study, diatomite was subjected to extrusion, sintering and granulation to form diatomaceous earth particles that were further modified via chitosan aminomethylation for modification. FTase derived from Aspergillus oryzae was successfully immobilized on the modified support via covalent binding.RESULTSThe immobilized enzyme activity was 503 IU g-1 at an enzyme concentration of 0.6 mg mL-1, immobilization pH of 7.0 and contact time of 3 h. Additionally, the immobilization yield was 56.91%. Notably, the immobilized enzyme was more stable under acidic conditions. Moreover, the half-life of the immobilized enzyme was 20.80 and 10.96 times as long as that of the free enzyme at 45 and 60 degrees C, respectively. The results show good reusability, as evidenced by the 84.77% retention of original enzyme activity after eight cycles. Additionally, the column transit time of the substrate was 35.56 min when the immobilized enzyme was applied in a packed-bed reactor. Furthermore, a consistently high FOS production yield of 60.68% was achieved and maintained over the 15-day monitoring period.CONCLUSIONSOur results suggest that immobilized FTase is a viable candidate for continuous FOS production on an industrial scale. (c) 2024 Society of Chemical Industry.

As the utilization of maltodextrins in food, pharmaceuticals, and agriculture continues to expand, substantial research has been conducted to enhance their functionality. Among the methods presented, the one-pot approach for the synthesis of nonreducing maltoheptaose offers a novel solution to the challenge of maltodextrins with varying degrees of polymerization and reducing ends. Nevertheless, the key enzyme in this method was currently only expressed in Escherichia coli , which restricts the applicability of this method in the food and pharmaceutical industries. In this study, the food-grade expression of cyclomaltodextrinase (CDase, EC 3.2.1.54), one of the key enzymes, was achieved using Bacillus subtilis as a host. The enzymatic properties of the recombinant CDase were then investigated, and the extracellular secretion of the CDase was enhanced in order to make it more widely available for use in the food industry. The enzyme exhibited optimal activity at a pH of 8.0 and a temperature range of 35 -45 degrees C. After incubation at 25 -35 degrees C for 10 h, 90% of the enzyme activity was retained. Additionally, the enzyme retained 80% of its initial activity after 24 h at pH 5.5 -9.5. Finally, Cu 2+ completely inhibited the enzyme activity. The extracellular secretion efficiency of recombinant CDase was significantly increased by the addition of Mn 2+ to the fermentation medium. The percentage of extracellular enzyme activity increased to 63.75% when the final concentration of Mn 2+ in the fermentation medium was 5 mM, which was 5.3-fold higher than that of the unadded one.

Kelp (Laminaria japonica) is rich in resources and a variety of active substances. However, its fishy flavor, which is hard to remove, poses challenges to consumer preferences. This study investigated the removal of fishy odor from Saccharomyces cerevisiae SK1.008 fermented kelp and kelp treated with fermentation combined natural antioxidant soaking through gas chromatography-mass spectrometry (GC-MS), odor activity values (OAVs) and gas chromatography-ion mobility spectrometry (GC-IMS). A total of 79 and 72 substances were identified in kelp using GC-MS and GC-IMS analysis, respectively. There were 16 volatile compounds (VOCs) with OAV>1 which were identified as key contributors to fishy odor, including (E,Z)-2,6-nonadienal, 1-octen-3-one, (E,E)-2,4-octadienal, (E,E)-2,4-decadienal and (E)-2-nonenal et al. The GC-MS analysis revealed that the removal efficiency of unsaturated aldehydes and ketones was 73.3% in kelp treated by fermentation combined soaking. The hierarchical cluster analysis and principal component analysis (PCA) constructed by GC-IMS revealed that the blank kelp, fermented kelp and kelp treated with fermentation combined soaking can be distinguished by volatile compounds. This study provides a reference for establishing a long-term effective deodorization method.

Cold-pressed sugarcane juice (SCJ) is a beverage rich in vitamins, carbohydrates, and antioxidants. Various sterilization methods impact fruit juice's appearance, nutrients, and flavor. Hence, this study aims to assess how different sterilization techniques affect the flavor, appearance, and nutritional value of SCJ. Freshly prepared SCJs were subjected to two sterilization methods: pasteurization (referred to as PTG) and autoclaving (referred to as HTHP). The pasteurization process was carried out at 63°C for 30 min, whereas the HTHP process was applied at 115°C for 30 min. The appearances, Brix value, colors, sugar, organic acid content, and aromatic compounds were determined. The Brix and pH values of the juice show little variation across different heat treatments. The color index of PTG was similar to that of the control group, whereas the L* value of HTHP increased about 21%, resulting in a significant color change. The glucose and fructose contents of HTHP were 7.03 and 5.41 mg/mL, which were much higher than those of PTG (3.26 and 2.33 mg/mL) and control group (3.33 and 2.48 mg/mL). A total of 77 aromatic compounds were identified in the SCJ after various heat treatments. Among them, pentanoic acid, octanal, and β-damascenone were the most abundant substances contributing to the overall flavor in the control group, PTG, and HTHP. Pasteurization preserved the original flavor of the juice, whereas autoclaving triggered the Maillard reaction, forming pyrazine and furan-like compounds that altered the SCJ's flavor. In conclusion, pasteurization retained SCJ's original characteristics, whereas HTHP induces changes in nutrition and imparts a distinct flavor.