Soybean Isolate Research Articles

Performance comparison of anthocyanin-based smart indicator films

Anthocyanins are natural dyes from plants that change color according to environmental changes, allowing for their potential use in real-time freshness-indicator films. In this study, black rice extract (BRE), black soya bean extract (BSBE), black wolfberry extract (BWE), purple sweet potato extract (PSPE), purple cabbage extract (PCE) and roselle extract (RE) were added to soybean isolate protein/chitosan (SPI/CS) films, and their performance was assessed. Results showed the total anthocyanin content of these six extracts were 1.50, 1.13, 1.98, 0.47, 0.33, 2.67 mg/mL, respectively. The presence of the six major anthocyanins was confirmed by mass spectrometry. Spectroscopy revealed that anthocyanin addition did not induce interactions between the extracts and SPI/CS film. Excess of anthocyanins weakened interactions between macromolecules, damaged membrane structure and reduced mechanical properties. Membrane water barrier properties improved with an increase in anthocyanin content, as well as antioxidant properties, but the difference between the indicator films was not significant. Finally, SPI/CS/RE exhibited a significant color change and the sensitivity was up to 50.6%, indicating the best application performance.

Effect of palm oil content and melting point on the freeze-thaw stability of fat substitutes

Animal or plant-based meat products are typically stored and transported using freezing. Freezing-thawing cycles can lead to detrimental changes in the texture, appearance, and mouthfeel of fat substitutes, thus affecting their quality. In this work, a protein/polysaccharide composite emulsion gel was created by emulsifying soybean isolate protein (SPI) and palm oil (PO), and incorporating curdlan (CL). It can serve as a potential replacement for animal fat in meat products, such as sausage, and plant-based meat. The study aimed to investigate the stability of the complex fat substitutes during freeze-thaw at various melting points and palm oil content. The results showed that the 52°C-palm oil samples were the most freeze-thaw stable compared to samples with other melting points. 52°C-palm oil samples were tested for texture and water holding capacity (WHC), increasing the oil content from 5g/100g–20g/100g improved the gel strength and WHC after freeze-thaw. The samples containing high melting point palm oil were less affected by temperature changes and showed higher stability as detected by low-field NMR and differential calorimetric scanning. The confocal laser scanning and rheological detection further confirmed the enhanced structural strength and freeze-thaw stability of the emulsion gels containing solid fat particles with high melting points.

Assembly of soy protein-corn starch composite gels by thermal induction: Structure, and properties

The effect of different corn starch (CS) concentrations on the gel formation of soybean isolate protein (SPI) was investigated. Moreover, the texture, rheological properties of the gel were determined, and the spatial structure and interactions of the composite gel system were analyzed. The composite system transitioned from liquid to solid-like with an increase in the CS concentration and did not backflow when inverted for 24 h. With the addition of CS, the gel strength, water holding capacity (WHC), G′, and G′′ increased significantly. The maximum was reached at 10 % starch concentration with gel strength of (228.96 ± 29.86) g and WHC of (98.93 ± 2.02) %. According to low-field 1H nuclear magnetic resonance (LF-NMR) results, CS has a high water absorption capacity, which improved the WHC. The scanning electron microscopy results revealed that composite gels with a high CS concentration had a more dense and small void network structure. According to the results of molecular force interaction, infrared spectroscopy, Raman spectroscopy, and free sulfhydryl group analysis, the added starch promoted the unfolding of SPI molecules, exposure of hydrophobic groups, transformation of free sulfhydryl groups into disulfide bonds, and hydrogen bond formation. Hydrophobic interactions, disulfide bonding, and hydrogen bonding function together to form the SPI–CS composite gel system. The study results provide the basis for applying soy protein and CS gels.

Changes in the structure and functional properties of soybean isolate protein: Effects of different modification methods

Soybean protein isolate (SPI) is an important plant protein in food processing; however, its spherical structure prevents the exposure of its hydrophobic residues and affects its functional properties. In this study, we elucidate the effects of deamidation, phosphorylation, and glycosylation on the structure (Fourier-transform infrared spectroscopy, circular dichroism, fluorescence, and scanning electron microscopy) and functional properties (solubility, emulsifying activity index (EAI), and emulsifying stability index (ESI)) of SPI. The zeta potentials of the deamidated, phosphorylated, and glycosylated (DSPI, PSPI, and MSPI, respectively) samples decreased significantly (p < 0.05) relative to those of SPI. The functional properties of the modified SPI samples were improved, with MSPI-2 showing the best solubility (86.73 ± 0.34%), EAI (118.89 ± 0.73 m2/g), and ESI (273.33 ± 0.59 min). Moreover, the effects of the three modifications on the SPI functional properties increase in the order MSPI > PSPI > DSPI. These results provide a theoretical understanding the relationship between the modifications and SPI structure.

Fabrication of nanoemulsion stabilized by high-pressure modified soy protein isolate-genistein for the encapsulation of lutein

In this study, we evaluated the interaction between high-pressure homogenization modified soybean isolate protein (HSPI) and genistein (GE), and constructed nanoemulsions for the co-encapsulated of GE and lutein using HSPI-GE as emulsifier. SPI formed complexes with GE mainly through hydrophobic interactions, and high-pressure homogenization treatment improved the interaction between SPI and GE. When the homogenization pressure was 120 MPa, the emulsification activity and emulsion stability indexes of HSPI-GE reached 196.71 m2g-1 and 237.98min, and the zeta potential of HSPI-GE nanoemulsion was −34.15 mV. Additionally, the encapsulation efficiency of HSPI-GE nanoemulsion was up to 93.88% and its storage stability was up to 66.01% after 20 d of storage. The HSPI-GE nanoemulsions achieved slow release of co-encapsulated GE and lutein and improved their bioaccessibility to 74.47% and 80.46% in in vitro simulated digestion. This work provides a theoretical basis for further studies on the application of HSPI-GE in lutein delivery systems.

Effect of Freezing on Soybean Protein Solution.

To investigate the impact of frozen storage conditions on the physicochemical properties of soybean protein and explore the underlying mechanisms, this study focused on soybean isolate (SPI), ß-soybean companion globulin (7S), and soybean globulin (11S). The protein solutions were prepared at a concentration of 2% and subjected to freezing for 1 and 5 days. Subsequently, the protein content, physicochemical properties, secondary structure, sulfhydryl content, and chemical interaction forces were assessed and analyzed using UV spectrophotometry, Zeta potential measurements, SDS-PAGE, Fourier infrared spectroscopy, and endogenous fluorescence photoemission spectroscopy. The obtained results revealed that the solubility and total sulfhydryl content of SPI, 7S, and 11S exhibited a decreasing trend with prolonged freezing time. Among them, 11S demonstrated the largest decrease in solubility and total sulfhydryl content, followed by SPI, and 7S the least. During freezing, the aromatic amino acids of SPI, 7S, and 11S molecules were exposed, leading to increased hydrophobicity, protein aggregation, and particle size enlargement, and the structure of the protein changed from disordered structure to ordered structure. After freezing, the polarity of the microenvironment of SPI, 7S, and 11S increased, and their maximum fluorescence emission wavelengths were red-shifted. Notably, the largest red shift of SPI was from 332 nm to 335 nm. As freezing time increased, the contribution of hydrogen bonding increased, while the contribution of hydrophobic interactions decreased. This indicates that freezing affects the hydrophobic interactions, hydrogen bonding, and other chemical forces of the protein. The growth of ice crystals leads to the unfolding of protein molecular chains, exposure of internal hydrophobic groups, enhancement of hydrophobicity, and alters the secondary structure of the protein.

Storage-Induced Changes in Plasticizer Emigration and Structural Properties of Soybean Isolate Protein-Based Composite Films

Storage-Induced Changes in Plasticizer Emigration and Structural Properties of Soybean Isolate Protein-Based Composite Films

Fabrication and characterization of succinylated and glycosylated soy protein isolate and its self-assembled nanogel

In this study, we used succinic anhydride (SA) acylation and dextran (DX) glycosylation modified soybean isolate protein (SPI) to develop self-assembled SPI-SA-DX adduct-based nanogels. Degree of modification, SDS-PAGE, and FT-IR studies showed that the amino group of the SPI was replaced by hydrophilic dextran and succinic acid carboxyl groups. Dextran chain and anhydride group attachment to the soybean protein surface enhanced hydrophilicity and spatial site blocking. Modification-induced protein structure unfolding, free sulfhydryl groups to be converted to disulfide bonds, and reduced surface hydrophobicity (H0). H0 was lowest at 33,750 ± 1008.29 when SA content = 10 % protein content (SPI-SA3-DX). The nanometer gel based on SPI-SA3-DX had the maximum turbidity and clear transparent solution without precipitation. Its particle size and polymer dispersibility index (PDI) were also the smallest, with values of (106.87 ± 4.51) nm and 0.21 ± 0.009, respectively. Transmission electron microscopy showed that nanogels had subspherical shell-core structures. Nanogels were stable under different pH, ionic strength, high temperature, and storage conditions.

Use of the sludge obtained from the electrocoagulation process of pumping waters of fishmeal factories for feeding Tenebrio molitor larvae

Sludge residue from pumping water treatment obtained by electrocoagulation process (LEC) in fishmeal factories, was used as a feeding ingredient for Tenebrio molitor larvae. LEC was conditioned by three bioprocesses: fermentation with Lactobacillus casei, fermentation with Sacharomyces, and hydrolysis with pancreatin enzymatic mixture. Soybean isolate was used as a control. Larvae consuming LEC-containing diets presented a higher weight gain rate than the controls. The proximal larvae dry basis composition values of fat, ash, and protein (37.2% ± 2%, 3.9% ± 0.4%, and 50.2% ± 4.9%, respectively) did not present significant intergroup differences. LEC contained 4.2% aluminum and its conditioning through fermentation with lactic bacteria reduced its bioavailability in the larvae, with values similar to those of controls (3.9 ± 0.7 μg Al/g). The iron content in LEC-fed larvae was higher than that in the control group, while their fatty acid profile was only slightly different. These initial results with LEC, which organic material is difficult to hydrate and assimilate, suggest its suitability as a protein source and attractant for a faster growth of T. molitor larvae.

Acid-Mediated Formation of Soybean Isolate Protein Emulsion Gels with Soybean Oil as an Active Component.

In this study, the effect of soybean oil concentration on the rheology, water-holding capacity, and thermal stability of acid-mediated soy protein isolate (SPI) emulsion gels was investigated. The microstructure was analyzed and interpreted by CLSM and SEM observations. The results showed that the addition of soybean oil improved the elastic properties of the acid-mediated SPI emulsion gels. The storage modulus increased from 330 Pa (2% soybean oil concentration) to 545 Pa (8% soybean oil concentration) with a significant increase (p < 0.05). The increase in soybean oil concentration resulted in more SPI-coated oil droplets acting as active particles, enhancing the gel network. The acid-mediated SPI emulsion gels became more disordered as the soybean oil concentration increased, with the fractal dimension increasing from 2.92 (2%) to 2.95 (8%). The rheological properties, thermal analysis, and microstructure of 6% SPI gel and acid-mediated SPI emulsion gels with 2% to 8% soybean oil concentration were compared. The acid-mediated SPI emulsion gels with soybean oil as the active filler showed improved gel properties, greater thermal stability, and a homogeneous network structure compared to the acid-mediated SPI emulsion gels.

Study on the Structure, Function, and Interface Characteristics of Soybean Protein Isolate by Industrial Phosphorylation

The impacts of industrial phosphorylation on the structural changes, microstructure, functional, and rheological features of soybean protein isolate (SPI) were spotlighted. The findings implied that the spatial structure and functional features of the SPI changed significantly after treatment with the two phosphates. Sodium hexametaphosphate (SHMP) promoted aggregation of SPI with a larger particle size; sodium tripolyphosphate (STP) modified SPI with smaller particle size. SDS-polyacrylamide gel electrophoresis (SDS-PAGE) results showed insignificant alterations in the structure of SPI subunits. Fourier transform infrared (FTIR) and endogenous fluorescence noted a decline in α-helix quantity, an amplification in β-fold quantity, and an increase in protein stretching and disorder, indicating that phosphorylation treatment fluctuated the spatial structure of the SPI. Functional characterization studies showed that the solubility and emulsion properties of the SPI increased to varying degrees after phosphorylation, with a maximum solubility of 94.64% for SHMP-SPI and 97.09% for STP-SPI. Emulsifying activity index (EAI) and emulsifying steadiness index (ESI) results for STP-SPI were better than those for SHMP-SPI. Rheological results showed that the modulus of G' and G″ increased and the emulsion exhibited significant elastic behavior. This affords a theoretical core for expanding the industrial production applications of soybean isolates in the food and various industries.

Purification and characterization of aspartic protease from Aspergillus niger and its efficient hydrolysis applications in soy protein degradation

BackgroundAdding acid protease to feed can enhance protein digestibility, boost feed utilization, and stimulate the growth of animals in breading industry. In order to obtain an acid protease with high hydrolysis efficiency to plant protein, in this study, an aspartic protease from Aspergillus niger was heterologous expressed in Pichia pastoris (P. pastoris). The enzymatic properties and application in soybean protein degradation were also studied.ResultsIn our investigation, the high aspartic protease (Apa1) activity level of 1500 U/mL was achieved in 3 L bioreactor. After dialysis and anion exchange chromatography, the total enzyme activity and specific enzyme activity were 9412 U and 4852 U/mg, respectively. The molecular weight of the purified protease was 50 kDa, while the optimal pH and temperature were 3.0 and 50 °C, respectively. It was stable at pH 2.0–5.0 and 30–60 °C. Apa1 was used to hydrolyze soybean isolate protein (SPI) at 40 °C and pH 3.0, and a high hydrolysis degree (DH) of 61.65% was achieved. In addition, the molecular weight distribution of SPI hydrolysis products was studied, the result showed that the hydrolysis products were primarily oligopeptides with molecular weights of 189 Da or below.ConclusionsIn this study, Apa1 was successfully expressed in P. pastoris and high expression level was obtained. In addition, the highest protein hydrolysis rate to SPI degradation so far was achieved. The acid protease in this study provides a new protease that is suitable for the feed industry, which will be very helpful to improve the feed utilization and promote the development of the breeding industry.

A Charge Equalizer in Accordion—MXene‐Modified Layer Leading to Spherical Lithium Deposition

Lithium‐ion batteries with polymer electrolytes (PEs) are promising candidates for high safety performance batteries. However, conventional PEs suffer from poor compatibility and high impedance of electrolyte–electrode interfaces. Herein, we present a method of the interfacial modification for PEs to inhibit lithium dendrites based on the solution to the interfacial compatibility. Our strategy is to improve the interfacial properties and inhibit the dendrite generation by coating a modified layer on PEs of the anode side with acetylene black (AB) and MXene. The mixed conductive layer (MCL) can promote the generation of Li3N and LiF with a uniform arrangement of electrons to form a dense solid electrolyte interphase layer and the even lithium‐ion deposition for improving the performance and stability of the battery during cycling. After adding the MCL, the discharge capacity of solid lithium‐ion batteries (SLIBs) with lithium bis(trifluoromethanesulfonyl)imide (LiTFSI)/organic modified montmorillonite (OMMT)/soybean isolate protein (SPI)/poly(vinylidene fluoride) (PVDF) (LOSP) PE from 74.2 mAh g−1 up to 111.1 mAh g−1 (AB‐LiTFSI/OMMT/SPI/PVDF (AB‐LOSP)) and 111.6 mAh g−1 (AB/MXene‐LiTFSI/OMMT/SPI/PVDF (AB/MXene‐LOSP)). The polarization voltage dropped by 0.06 and 0.12 V, respectively. This work represents a milestone in the dendrite‐free SLIBs with good performances.

The structural and functional properties of soybean protein-polyglutamic acid complex effected the stability of W/O/W emulsion encapsulated Nattokinase

Nattokinase (NK) derived from food is a sustainable thrombolytic agent. In this study, to protect vulnerable biological activity of NK, the targeted modified W/O/W emulsions were fabricated from complexes of soybean isolate protein (SPI) and polyglutamic acid (PGA). The results showed that the SPI-PGA complex formed a tighter internal structure through non-covalent bonds. The secondary structure, α-helix and β-sheet content of the 1:3 (v/v) ratio complex of SPI to PGA increased by 6.14% and 8.62%, respectively. The emulsification and stability of the complexes were improved by refining structural properties as against SPI. The W/O/W emulsions coated by complexes formed the stronger network structure with higher encapsulation efficiency, better interfacial features, and better storage stability. Moreover, the highest bioavailability was achieved by W/O/W emulsions coated with 1:3 ratio complex at 80.69%. This study provided a new strategy towards tailoring ideal emulsion vehicles and expanded the NK application in food formulations.

Effects of rice protein, soy isolate protein, and whey concentrate protein on the digestibility and physicochemical properties of extruded rice starch.

Protein, as the second major component in starchy foods, is crucial for its influence on the physicochemical properties and digestibility of starch. However, the effect of different sources of protein on starch digestibility is still unclear. In this paper, the effects of different sources of proteins (rice protein: RP, soybean isolate protein: SPI, and whey concentrate protein: WPC) on structural features, digestibility, and enzyme activity of extruded rice starch were investigated. The addition of all three proteins reduced the starch digestibility of extrudates. Native SPI and WPC suppressed amyloglucosidase activity, and all three proteins exhibited stronger amyloglucosidase inhibition when hydrolyzed. The rheological properties and Fourier transform infrared spectroscopy results revealed the exogenous proteins and starch interacted through non-covalent bonds and improved the ordered structures in the extrudates. The extrusion process also facilitated the formation of a V-type structure. The sum of SDS and RS content of extrudates was negatively correlated with the content of leached amylose and positively correlated with the ratio of 1047/1022cm-1 . These findings suggest that the inclusion of exogenous proteins during extrusion can affect starch digestibility through mechanisms such as the interaction with starch molecules, as well as the inhibition of amylase activity. PRACTICAL APPLICATION: This result indicated that the addition of protein during extrusion not only increased the nutritional value of the extrudate, but also decreased the starch digestibility. Extrusion technology can efficiently produce extruded products with protein, expanding further applications of protein in food and providing new healthy staple food options for special populations, such as diabetic and overweight people.

Functional properties of soybean isolate protein as influenced by its critical overlap concentration

The critical overlap concentration (c*) of soy protein isolate (SPI) was studied at a wide range of temperatures (10–90 °C). Results obtained indicate that temperature and c* were directly proportional. The c* determined experimentally was similar to the theoretical value that was calculated by the inverse of the intrinsic viscosity, [η]. At c*, SPI solutions can be divided into the dilute and semi-dilute regimes. The [η] values were estimated by four semi-empirical equations: the Huggins equation, the Kraemer equation, the Tanglertaibul-Rao equation, and the Oliver-Ward equation, of which the Oliver-Ward equation was found to be the most suitable. The aggregation behavior of the SPI was confirmed by association with the start of molecular entanglement at c*. Turbidity, foam capacity (FC) and foam stability (FS) increased significantly when solutions concentration reached c* at all experimental temperatures. The rheology measurement results indicated onset of gel formation when protein concentration reached c* at 90 °C, which can be considered as the gel formation concentration at that temperature. At concentrations below c*, the SPI solutions were unable to form gels and had much lower water holding capacities (WHC) than gels prepared at c*. These findings suggested that c* was related to a number of functional characteristics of SPI, including FC, FS and WHC, and can be used to estimate the concentration required for protein gel formation.

Hypoglycemic Activity of Self-Assembled Gellan Gum-Soybean Isolate Composite Hydrogel-Embedded Active Substance-Saponin.

In order to avoid hemolysis caused by direct dietary of kidney tea saponin, complex gels based on gellan gum (GG) and soybean isolate protein (SPI) loaded with saponin were created in the present study by using a self-assembly technique. Studies were conducted on the rheological characteristics, encapsulation effectiveness, molecular structure, microstructure, and hypoglycemic activity of GG/SPI-saponin gels. Increasing the concentration of SPI helped to enhance the strength and energy storage modulus (G') of the gels, and the incorporation of high acylated saponin allowed the whole gel to undergo sol-gel interconversion. The encapsulation efficiency showed that GG/SPI-saponin was 84.52 ± 0.78% for saponin. Microstructural analysis results suggested that GG and SPI were bound by hydrogen bonds. The in vitro digestion results also indicated that saponin could be well retained in the stomach and subsequently released slowly in the intestine. In addition, the in vitro hypoglycemic activity results showed that the IC50 of encapsulated saponin against α-glucosidase and α-amylase were at 2.4790 mg/mL and 1.4317 mg/mL, respectively, and may be used to replace acarbose for hypoglycemia.

Effect of Storage Temperature on Physical Properties and Application in Packaging of the Soybean Isolate Protein–Corn Starch Composite Films

AbstractIn order to evaluate the stability of soybean isolate protein (SPI)–corn starch (CS) composite films, physical properties and application in packaging of the SPI‐based composite films are observed during storage. Results show that mechanical property changed more obvious (increased TS and descended EB) with increase of storage temperature from 5 to 35 °C and increased CS content in the SPI‐CS composite films is not in advantage of mechanical property improvement. Furthermore, combined with results of light transmittance, oil barrier property, and water solubility, it is obtained that low temperature (≤20 °C) is preferred for storage of SPI‐based composite films, and SPI:CS (4:1) composite film shows best performance during the whole storage. Finally, films applied in packaging result indicate the SPI:CS (4:1) composite film can be selected as seasoning inner packaging at low temperature.

The Effect of Different Induction Methods on the Structure and Physicochemical Properties of Glycosylated Soybean Isolate Gels.

Soybean protein isolate (SPI), as a full-valued protein, is rich in nutrients, such as amino acids. However, the isolated structure of soybeans makes it difficult to react and thus prepare good gels. In order to further improve the properties of SPIs and to prepare plant-based gels with good performance, this experiment was conducted to prepare maltodextrin glycosylated soybean isolate (MGSI) by the glycosylation of SPI and maltodextrin (MD), and the gels were prepared by thermal induction, transglutaminase (TGase) induction, and TG-MgCl2 co-induction of this glycosylated protein to investigate the effects of different induction methods on the structure and properties of the gels produced by MGSIs. Moreover, the effects of different induction methods on the structure and properties of the gels produced by MGSI were investigated. SDS-PAGE protein electrophoresis, FTIR spectroscopy, and endogenous fluorescence spectroscopy revealed that all three inductions result in the covalent bond cross-linking of MGSI during the gel formation process. Compared with thermal induction, the TGase-induced MGSI secondary structure had a higher content of β-folded structures, increased fluorescence intensity of tertiary structures, and produced a red shift. The gel induced by TGase in collaboration with MgCl2 contains a more β-folded structure and irregular curl and increases the β-turned angle and α-helix content further, the endogenous fluorescence λmax is significantly red-shifted, and the fluorescence intensity increases, demonstrating that the tertiary structure of MGSI unfolds the most, forming multilayered gels with the tightest structures. The three gels were analyzed by rheology and SEM, showing that the TGase-MgCl2 synergistically induced gel had the highest energy-storage modulus G', viscoelasticity, and water-holding capacity, as well as the densest gel structure. In conclusion, the combined treatment of enzyme and MgCl2 might be an effective way of improving the structure and gel properties of SPI. This study helps to promote the high-value utilization of SPI and the development of plant protein gels.

Pemanfaatan Tepung Pisang-Singkong Sebagai Alternatif Pengganti Tepung Terigu Pada Pembuatan Mie Dengan Penambahan Putih Telur atau Isolat Kedelai

In general, wheat flour noodles have a chewy and elastic texture, due to the presence of amylose, amylopectin and gluten proteins. People with celiac disease are gluten intolerant, so to enjoy noodles like people in general, an alternative gluten-free flour is needed to replace wheat flour, one of which is banana-cassava flour. To increase the nutritional value and texture of noodles, such as using wheat flour, egg white protein or soybean isolate and xanthan gum or ash water are added. This study aims to determine the effect of adding egg white protein or soybean isolate and the effect of xanthan gum or water ash on banana-cassava flour noodles on the physicochemical and sensory profiles. The research stages are the production of banana-cassava flour noodles, physicochemical profile analysis includes chemical profiles (moisture content, ash content and protein content), physical profile (optimum cooking time, swelling index, cooking loss and water absorption) and gluten content and sensory testing. The results of the analysis showed that the chemical profile of banana-cassava flour noodles met the wet noodle quality standard set by SNI 2987-2015, while the ash content was higher than the quality standard. Some good formulas, the water and ash content in the addition of egg white and xanthan gum (PTX) were around 4.95% and 1.80%, respectively, while the protein content in the addition of soybean isolate and water ash (PKA) was 12.89%. . Physical profiles for cooking time and swelling index on the addition of soybean isolate and water ash (PKA) were 2.50 minutes and 186.10%, respectively, cooking loss on the addition of egg white and xanthan gum (PTX) was 5.85%, while the water absorption in the addition of egg white and water ash (PTA) was 73.95%. Gluten levels in the addition of soybean isolates and water ash (PKA) ranged from 1.10%. The physicochemical profile of banana-cassava flour noodles was influenced by the type of protein and the best formula for gluten-free noodles was the addition of soy isolate. While the ash content, swelling index, water absorption, and gluten content are influenced by the type of agglomerate, and the best formulation for gluten-free noodles is the addition of ash water. The results of the organoleptic test obtained an average score of 4 (out of a scale of 5) on the attributes of color, aroma, taste, texture, and overall preference for the banana-cassava flour noodle sample.