Preparation Of Hydrolysates Research Articles

Hydrolysates of mare's milk proteins. Immunochemical and physico-chemical characteristics

In recent years, the attention of specialists has been attracted by a significant increase in allergic diseases, especially among children. Enzymatic hydrolysis with the participation of peptidases is considered the most effective measure to reduce the allergenicity of milk proteins. The study of the features of protein proteolysis by various enzymes, aimed at establishing optimal process parameters, is the subject of research in the production of hydrolysates with specified properties: a certain peptide and amino acid profile, reduced antigenic properties. At the same time, for a correct preclinical assessment of the safety and potential effectiveness of specialized food products, it is not enough only to determine the molecular weight distribution of peptide fractions in the composition. A necessary additional and informative indicator of reducing the potential allergenicity of the hydrolysate is the degree of preservation of the antigenic properties of the initial protein (residual antigenicity), determined by immunochemical methods. The preparation and subsequent comprehensive assessment of enzymatic hydrolysates of mare's milk proteins is of considerable interest, since, according to the results of clinical studies, it was suggested that upon allergy to cow's milk proteins mare's milk can be considered hypoallergenic. The purpose of this work was to obtain enzymatic hydrolysates of mare's milk proteins using domestic enzymes and their further physico-chemical and immunochemical characteristics. The object of the study was mare's milk protein obtained from skimmed mare's milk powder as a protein substrate. Two samples of enzymes from various manufacturers of the Russian Federation were used in the work. The results of the conducted studies show that the peptide profiles of hydrolysates vary greatly depending on the enzyme used, however, the multiplicity of antigenicity reduction practically does not depend on the nature of the enzyme, and does not depend on an increase in the enzyme/substrate ratio. The peptide profile and the multiplicity of reducing the antigenicity of hydrolysates of mare's milk proteins are influenced by ultrafiltration treatment of the obtained hydrolysates, which allows reducing the content of antigenic structures in the final product by several orders of magnitude.

Characteristics and Bioactivities of Protein Hydrolysate from Cricket (Acheta domesticus) Powder Defatted Using Ethanol with Aid of Vacuum Impregnation.

Cricket is a potential proteinaceous source used for protein hydrolysate (PH) preparation, having several biological activities. Nevertheless, cricket has high lipid contents, which are susceptible to oxidation during PH preparation. Thus, ethanol was used together with vacuum impregnation (VI) to enhance defatting efficacy before PH preparation. Also, bioavailability of the digest of PH after gastrointestinal tract (GIT) digestion via the Caco-2 monolayer was assessed. Cricket powder was defatted using ethanol for 1-4 h. Lipid contents were decreased with enhancing time until 2 h. Additionally, the defatting efficacy was augmented when ethanol combined with VI at 4 cycles for 2 h (VI-E-2) was implemented. Lowered mono- and polyunsaturated fatty acid contents were also observed in the VI-E-2 sample. The VI-E-2 sample was used to prepare PH using Alcalase and Flavourzyme (0.2-0.4 units/g dry sample). PH prepared by Alcalase hydrolysis at 0.2 units/g dry sample (A-0.2) showed the higher ABTS radical-scavenging activity and FRAP, compared to that prepared by Flavourzyme hydrolysis (p < 0.05). Thus, the A-0.2 sample was selected for digestion via the GIT system. The obtained digest (500-1000 μg/mL) had bioavailability of peptides, depending on the levels used. Therefore, PH from defatted cricket powder could be a promising ingredient for food applications.

Characterization of the extracellular proteases from Bacillus inaquosorum strain E1-8 and its application in the preparation of hydrolysates from plant and animal proteins with antioxidant, antifreeze and anti-browning properties.

Bacillus inaquosorum strains is widely recognized for their plant-growth-promoting and biocontrol capabilities, yet their roles in protease production remain unclear. The present study aimed to comprehensively assess the protease-producing performance of B. inaquosorum strain E1-8, at the same time as exploring the novel application of agricultural Bacillus proteases in the preparation of protein hydrolysates for fresh-cut fruits preservation. First, genomic sequencing revealed the diversity of E1-8 proteases, indicating 15 putative extracellular proteases. Subsequently, the fermentation conditions for E1-8 protease production were optimized, with sweet potato powder and soybean meal identified as the most suitable carbon and nitrogen sources, respectively, resulting in a maximum protease activity of 321.48 U mL-1. Upon culturing the strain under these optimized conditions, only an S8 family serine protease and an M48 family metalloprotease were revealed by secretomic analysis and protease inhibitor assays. Additionally, the optimal protease conditions for generating protein hydrolysates from soy, pea, fish and porcine proteins were determined. The molecular weight of the hydrolysates primarily ranged from 2000 to 180 Da, with a total of 17 amino acids identified. The application of these hydrolysates demonstrated a 2,2-diphenyl-1-picrylhydrazyl (i.e. DPPH) scavenging activity ranging from 58.64% to 84.12%, significantly reducing of the melting peaks and the freezing points. Furthermore, the browning index of apple slices stored at 4 °C decreased by 14.81% to 22.15% on the second day, and similar effects were observed in fresh-cut banana stored at 4 °C for 7 days. The protein hydrolysates obtained exhibit remarkable antioxidant, antifreeze and anti-browning properties for fresh-cut fruits. © 2024 Society of Chemical Industry.

Effect of Chicken Feather Hydrolysate on Growth of Spinach through Soil Amendment Method: Unraveling A Potential Liquid Biofertilizer

The study aims to investigate the effectiveness of chicken feather hydrolysate for promoting the growth of Spinacia oleracea L., a commonly consumed leafy green vegetable. An earlier isolated and identified keratinolytic bacterial species Bacillus tropicus was utilized for the preparation of chicken feather hydrolysate through submerged fermentation. Minimal media which was supplemented with chicken feather was used for the preparation of hydrolysate. The bacterial strain degraded chicken feather within 4 days of incubation after which the feather hydrolysate was collected and tested to check plant growth promoting activity through the seed germination trials and greenhouse study. Upon characterization of feather hydrolysate, it was found that the hydrolysate was a cocktail of Nitrogen, Phosphorus and Potassium (NPK) as well as other micro elements needed for plant growth. Four different concentrations of feather hydrolysate were employed for both the seed germination and greenhouse study which ranged from 25% (v/v), 30% (v/v), 35% (v/v) and 40% (v/v) including a control group (CN) which was not supplemented with feather hydrolysate. The hydrolysate supplementation brought about plant growth in all the four test concentrations with 35% (v/v) giving the highest result of 14 cm and 27.6 mg/g for tested parameters like plumule length and total chlorophyll content, respectively. The same concentration supported maximum seed germination and highest radicle extension for the germination studies as well. This study investigates the efficacy of chicken feather hydrolysate in promoting spinach growth, elucidating its potential as a fertilizer.

The rolling-disc milling texture-sorting of raw straw facilitates the reduction of steam explosion intensity

Lignocellulosic fermentable sugars have been attracting increasing attention due to the developments of synthetic biology, yet the heterogeneity of the raw material results in high pretreatment intensities and the generation of numerous fermentation inhibitors. In this study, the rolling-disc milling texture-sorting was established for raw material to mitigate inhibitors generation at its source, specifically targeting the variances in mechanical strength among corn straw tissues. Through the texture-sorting of raw corn straw, the low modulus of elasticity tissues in corn straw were crushed into soft-texture sorts and the high-strength tissues were retained as hard-texture sorts. The results showed that the steam explosion pretreatment intensity required for soft-texture sorts decreased by 77.34 %, from 1125.96 (180 °C, 5 min) to 255.10 (160 °C, 5 min), compared to the hard-texture sorts. The concentrations of inhibitors in the enzymatic hydrolysate of soft-texture sorts decreased by 55.10 %, from 8.13 g/L/(100 g/L total sugars) to 3.65 g/L/(100 g/L total sugars), indicating an improved suitability for enzymatic hydrolysate preparation. Therefore, the rolling-disc milling texture-sorting method was proposed to provide a new approach for the preparation of lignocellulosic fermentable sugars.

Characterisation and comparison of enzymatically prepared donkey milk whey protein hydrolysates

This study evaluated the structural characteristics, processing properties, and antioxidant properties of hydrolysates prepared from donkey milk (DM) whey protein using different proteases (Alcalase, Neutrase, papain, and Flavourzyme). The results showed that enzymatic hydrolysis significantly increased hydrolysate solubility and reduced average particle size compared to those of DM whey protein. Neutrase and Flavourzyme hydrolysates exhibited higher degrees of hydrolysis (DH), along with elevated emulsification properties and surface hydrophobicity. The choice of protease influenced secondary and tertiary protein structures and amino acid composition. Enzymatic hydrolysis led to decreased molecular weight of DM whey proteins. Moreover, all hydrolysates exhibited higher fluorescence intensity at λmax compared to DM whey protein, implying distinct properties due to the varied impacts of the four proteases on DM whey protein structure. The preparation of hydrolysates from DM whey proteins using proteases contributes to the development of integrated-value DM products.

Food bioactive peptides: functionality beyond bitterness.

Bitter taste is an aversive taste because it is unconsciously associated with toxic compounds. However, a considerable variability in bitter sensitivity exists in those who have the genetic polymorphism for bitter taste receptors (TAS2Rs). Besides the oral cavity, TAS2Rs are present in many body tissues, including the gastrointestinal tract; therefore, they are crucial players both in the gustatory/hedonic system and in the homeostatic system, triggering numerous biological responses, including adipogenesis, carcinogenesis, or immunity. Bitter-tasting compounds are widely distributed in plant and animal foods and belong to many chemical classes. In this study, the evidence was reviewed on bitter peptides, considering the food sources, their formation in food under different processing and storage conditions and in the gastrointestinal tract during digestion, as well as their biological activities. Bitterness associated with peptides is due to the presence of hydrophobic amino acids in the C-terminus. The current literature mainly explores the enzymes and hydrolysis conditions, with the aim of reducing the formation of bitter peptides in hydrolysate preparation or food. Few studies highlight the bioactivity (namely, antihypertensive, antidiabetic, antioxidant, or immunity boosting), besides the bitterness. However, encapsulation of bitter peptides has been tentatively used to develop antihypertensive and antidiabetic supplements. In the era of personalized nutrition and precision medicine, the evidence available suggests the opportunity to use bitter bioactive peptides as functional ingredients in food. Such types of food may modulate a plethora of physiological mechanisms by targeting TAS2Rs in the gastrointestinal tract, thus modulating appetite sensations or gastrointestinal motility and discomfort according to individual nutritional needs and goals. More studies are needed to optimize the technological strategies to target TAS2Rs by bitter bioactive peptides, improve their stability in food, and validate the biological efficacy through well-designed in vivo studies.

Purification of Trypsin from Sardine (Sardina pilchardus) Viscera and Its Application in Preparation of Antioxidative Fish Protein Hydrolysates

Purification of Trypsin from Sardine (Sardina pilchardus) Viscera and Its Application in Preparation of Antioxidative Fish Protein Hydrolysates

A strategy to boost xanthine oxidase and angiotensin converting enzyme inhibitory activities of peptides via molecular docking and module substitution

Molecular docking and activity evaluation screened the dipeptide module GP with low xanthine oxidase (XOD) inhibitory activity and modules KE and KN with high activity, and identified them as low- and high-contribution modules, respectively. We hypothesized the substitution of low-contribution modules in peptides with high contributions would boost their XOD inhibitory activity. In the XOD inhibitory peptide GPAGPR, substitution of GP with both KE and KN led to enhanced affinity between the peptides and XOD. They also increased XOD inhibitory activity (26.4% and 10.3%) and decreased cellular uric acid concentrations (28.0% and 10.4%). RNA sequencing indicated that these improvements were attributable to the inhibition of uric acid biosynthesis. In addition, module substitution increased the angiotensin-converting enzyme inhibitory activity of GILRP and GAAGGAF by 84.8% and 76.5%. This study revealed that module substitution is a feasible strategy to boost peptide activity, and provided information for the optimization of hydrolysate preparation conditions.

Bioactive peptides as a novel strategy to prevent alcoholic liver injury.

Alcohol intake has become one of the leading risks to human health and wellness, among which acute and/or chronic alcohol-induced liver injury is a leading threaten, with few therapeutic options other than abstinence. In recent years, studies suggested that certain bioactive peptides from food sources could represent natural and safe alternatives for the prevention of alcoholic liver injury. Hence, this chapter focus on the advanced research on bioactive peptides exerting hepatoprotective activity against alcoholic liver injury. The main sources of protein, strategies for the preparation of hepatoprotective hydrolysates and peptides, underlying mechanisms of peptides on hepatoprotection, and possible structure-activity relationship between peptides and hepatoprotective activity were summarized and discussed, aiming to give a systematic insight into the research progress of hepatoprotective peptides. However, more efforts would be needed to give a clearer insight into the underlying mechanisms and structure-activity relationship before using hepatoprotective peptides as functional food ingredients or dietary supplements.

Tea (Camellia sinensis (L.) Kuntze) as an emerging source of protein and bioactive peptides: A narrative review.

Tea residues represent one of the major agricultural wastes that are generated after the processing of tea. They account for 21-28% of crude protein and are often discarded without the extraction of valuable proteins. Due to various bioactivity and functional properties, tea proteins are an excellent alternative to other plant-based proteins for usage as food supplements at a higher dosage. Moreover, their good gelation capacity is ideal for the manufacturing of dairy products, jellies, condensation protein, gelatin gel, bread, etc. The current study is the first to comprehend various tea protein extraction methods and their amino acid profile. The preparation of tea protein bioactive peptides and hydrolysates are summarized. Several functional properties (solubility, foaming capacity, emulsification, water/oil absorption capacity) and bioactivities (antioxidant, antihypertensive, antidiabetic) of tea proteins are emphasized.

Efficient preparation of oyster hydrolysate with aroma and umami coexistence derived from ultrasonic pretreatment assisted enzymatic hydrolysis

In the study, an efficient protease Neutrase®-Flavourzyme® (NF) was screened to prepare the umami-aroma flavor oyster hydrolysate. The effect of protease and ultrasonic pretreatment (UP) assisted by the optimal protease on the flavor substances was investigated. The results demonstrated that the optimal UP-NF (450 W) showed a higher amino acid nitrogen content of 0.34 g/100 mL compared to the NF, and 19 major aroma compounds including octanal, decanal, nonanal, benzaldehyde, 2-undecanone, and 1-octen-3-ol were obtained. Additionally, the free amino acid and fatty acid spectrum indicated that the formation of flavor compounds was primarily due to the oxidation of linoleic and linolenic acids and the degradation of amino acids. Furthermore, taste analysis proved that increased umami and saltiness resulted from the accelerated release of Glu, Asp and 5′-IMP. Overall, UP-NF proved to be an effective method for producing umami-aroma flavor, facilitating further processing of oyster products for the application.

The preparation, characterization and gastroprotective activity of fermented oyster hydrolysate

The preparation, characterization and gastroprotective activity of fermented oyster hydrolysate

Collagen hydrolysates from deer tendon: Preparation assisted with different ultrasound pretreatment times and promotion in MC3T3-E1 cell proliferation and antioxidant activities

In this study, the hydrolysates of deer tendons with antioxidant activity and promoting bone proliferation activity were prepared using ultrasound. The results indicated that ultrasound (60 min) treatment had noticeable effects on the structure and enzymolysis degree of collagen protein, including looser structure, less α-helix/β-turn, more hydrophobic groups, and a higher degree of hydrolysis in comparison with others. Besides, compared with unpretreated collagen hydrolysates (CPHs), the hydrolysates with ultrasound treatment (60 min) showed significant effects on bone proliferation (cell proliferation rate: 63.9 ± 4.8%), alkaline phosphatase activity (14.488 U/mg), and antioxidant activities (DPPH radical scavenging rate: IC50 =4.05 mg/mL and ferric ion reducing antioxidant power (FRAP): 0.17 mmol Fe2+/mg). CPHs (ultrasound 60 min) also could protect MC3T3-E1 cells from H2O2-induced damage by reducing the ROS and [Ca2+]i. Taken together, these results might provide a basis for the ultrasound-assisted preparation of potential antioxidant hydrolysates to be applied in the food industry.

Functional Properties and Proximate Analysis of Fish Waste Protein Hydrolysate Processed Using Enzymes

A huge production of fish and their processing waste give rise to by-products comprises up to 70% depending on the species, size and processing method. The waste includes visceral parts, head, frames, bones, skin and cut-offs are rich source of protein with high functional properties. It is generally discarded which is a wastage of nutrient source and leading to environmental issues. Therefore, it was aimed to utilized the by-products for maximum recovery of nutrients by enzyme hydrolysis method for the preparation of protein hydrolysate with the used of papain and pepsin for digestion following different hydrolysis conditions. With the hydrolysis of papain enzyme (1 to 6%), the protein content of finfish waste protein hydrolysate ranges from 19.17% ± 0.06 to 73.14% ± 0.08 and that of shellfish waste protein hydrolysate prepared with 5,10 and 15% papain enzyme showed 26.73% ± 0.04 to 40.4% ± 0.5 which is comparatively low. Whereas the highest protein content was observed in 1% pepsin enzyme treated finfish waste protein hydrolysate with 80.55% ± 0.07. Besides, the hydrolysates were composed of 6.91% ± 0.05 to 10.46% ± 0.05 (moisture content), 0.6% ± 0.01 to 2.4% ± 0.01 (ash content) and 0.02% ± 0.005 to 0.09% ± 0.005 (fat content). The hydrolysates were highly soluble ranges from 72.73% ± 0.05 to 93.83% ± 0.1 which indicates development of small size hydrophilic with highly solvated polypeptide particles. A reduced phenomena of foaming capacity and stability were observed in shellfish waste protein hydrolysate in contrast with finfish waste protein hydrolysate. Similar pattern was also resulted in emulsifying stability index. Whereas the emulsifying activity index was in the range of 6.15 ± 0.03 to 9.85 ± 0.07 m2/g. The water holding capacity of finfish and shellfish waste protein hydrolysate ranges from 3.4 to 4.23 gm/gm hydrolysate and 1.53 to 1.63 gm/gm hydrolysate respectively which is resulted by the difference in molecular weight of the peptide. The hydrolysates extracted from different sample with different enzyme and concentration at varying conditions were more or less similar ranges from 3.7 to 4.1 gm/gm protein hydrolysate (oil holding capacity). Hence, high protein content with good functional properties of the protein hydrolysate prepared with the utilization of fish waste is a positive impact on the attempt made to recover nutrient by enzymatic hydrolysis.

Enzymatic Preparation of Mushroom By-product Protein Hydrolysates (Mb-PPHs)

The excessive use of chemical fertilizers can cause severe environmental damage. In recent decades, the application of biostimulants to improve soil composition and stimulate plant growth has contributed significantly to environmental preservation. In this paper, we studied the production and characterization of an amino acid/peptide-enriched biostimulant using edible mushroom (Agaricus bisporus) by-products (tails and nonmarketable mushrooms) as raw materials and commercial proteases as hydrolytic agents. A single hydrolytic process using four different endoproteases, Alcalase®, L-450, Flavourzyme® or papain, and a sequential hydrolytic process using two proteases, an endoprotease and an exoprotease, Alcalase® + Flavourzyme® or L-450 + Flavourzyme), were conducted. A preevaluation of potential plant biostimulants was also carried out, testing the biostimulant capacity of single and sequential Mb-PPHs to stimulate maize seed germination and root growth, as well as the evaluation of the vigor index (VI), with very promising results.Graphical

Preparation of sunflower seed-derived umami protein hydrolysates and their synergistic effect with monosodium glutamate and disodium inosine-5'-monophosphate.

Sunflower seeds are rich in protein and can be an excellent raw material for the production of umami peptides. In this study, sunflower seed meal, which was defatted at a low temperature, was taken as the raw material, and proteins were separated, followed by hydrolyzation for 4h by flavourzyme® to obtain hydrolysates with strong umami intensity. These hydrolysates were deamidated using glutaminase to increase the umami intensity. The highest umami value of 11.48 was recorded for hydrolysates deamidated for 6h, and the umami intensity was determined. The umami hydrolysates mixed with 8.92mmol IMP + 8.02mmol MSG showed the highest umami value of 25.21. Different concentrations of ethanol were used for further separation of hydrolysates, and the highest umami value of 13.54 was observed for 20% ethanol fraction. The results of this study provide utilization method for sunflower seed meal protein and a theoretical basis for the preparation of umami peptides. PRACTICAL APPLICATION: A large number of sunflower seed meals after oil production are used as feed for livestock and poultry. Sunflower seed meal is rich in protein, and umami amino acid composition in sunflower seed meal is up to 25%-30%, which is potentially an excellent raw material for the production of umami peptides. The umami flavor and synergistic effect of obtained hydrolysates, with MSG and IMP, were analyzed in the present study. We intend to provide a novel way for utilization of protein from sunflower seed meal along with a theoretical basis for the preparation of umami peptides.

Development, characterization and in vivo zinc absorption capacity of a novel soy meal hydrolysate-zinc complexes.

Zinc is an essential trace element for the human body. Recently, a novel Zn-binding peptide, Lys-Tyr-Lys-Arg-Gln-Arg-Trp (PP), was purified and identified from soy protein hydrolysates with high Zn-binding capacity (83.21 ± 2.65%) by our previous study. The preparation of soy meal hydrolysates (SMHs)-Zn complexes is convenient and low-cost, while PP (Lys-Tyr-Lys-Arg-Gln-Arg-Trp)-Zn complexes have a higher coordination rate but a relatively high cost. The aim of this study was to investigate the effect of soy meal hydrolysates (SMHs)-Zn complexes on zinc absorption in mice model, and synthetic soy peptide (PP)-Zn complexes with high Zn-binding capacity were used as control. Firstly, SMHs were prepared by enzymolysis, and the PP (Lys-Tyr-Lys-Arg-Gln-Arg-Trp) were synthesized based on previous studies. The binding mechanism of soy hydrolysates and zinc was analyzed by spectral analysis. Furthermore, the cytotoxicity of the SMHs-Zn complexes was also studied using the CCK-8 method. The effect of zinc absorption was evaluated based on Zn content, total protein and albumin content, relevant enzyme system, and the PeT1 and ZnT1 mRNA expression levels. The result showed that zinc was bound with carboxyl oxygen and amino nitrogen atoms on SMHs, with hydrophobic and electrostatic interactions as auxiliary stabilizing forces. SMHs-Zn were proved to have great solubility and a small particle size at different pH values, and it showed a beneficial effect on Caco-2 cells growth. Moreover, it was proved that SMHs-Zn and PP-Zn could increase the levels of zinc and the activity of Zn-related enzymes in mice. SMHs-Zn possessed higher PepT1 and ZnT1 mRNA expression levels than PP-Zn in the small intestine. SMHs-Zn with a lower Zn-binding capacity had similar effects on zinc absorption in mice as PP-Zn, suggesting that the bioavailability of peptide-zinc complexes in mice was not completely dependent on their Zn-binding capacity, but may also be related to the amino acid composition.

Preparation of Hypoallergenic Whey Protein Hydrolysate by a Mixture of Alcalase and Prozyme and Evaluation of Its Digestibility and Immunoregulatory Properties.

Whey protein (WP) has nutritional value, but the presence of β-lactoglobulin (β-LG) and α-lactalbumin (α-LA) cause allergic reactions. In this study, hypoallergenic whey protein hydrolyate (HWPH) was prepared by decomposing β-LG and α-LA of WP using exo- and endo-type proteases. The enzyme mixing ratio and reaction conditions were optimized using response surface methodology (RSM). Degradation of α-LA and β-LG was confirmed through gel electrophoresis, and digestion, and absorption rate, and immunostimulatory response were measured using in vitro and in vivo systems. Through RSM analysis, the optimal hydrolysis conditions for degradation of α-LA and β-LG included a 1:1 mixture of Alcalase and Prozyme reacted for 10 h at a 1.0% enzyme concentration relative to substrate. The molecular weight of HWPH was <5 kDa, and leucine was the prominent free amino acid. Both in vitro and in vivo tests showed that digestibility and intestinal permeability were higher in HWPH than in WP. In BALB/c mice, as compared to WP, HWPH reduced allergic reactions by inducing elevated Type 1/Type 2 helper T cell ratio in the blood, splenocytes, and small intestine. Thus, HWPH may be utilized in a variety of low allergenicity products intended for infants, adults, and the elderly.

Production efficiency and properties of bacterial cellulose membranes in a novel grape pomace hydrolysate by Komagataeibacter melomenusus AV436T and Komagataeibacter xylinus LMG 1518

The microbial production of cellulose using different bacterial species has been extensively examined for various industrial applications. However, the cost-effectiveness of all these biotechnological processes is strongly related to the culture medium for bacterial cellulose (BC) production. Herein, we examined a simple and modified procedure for preparing grape pomace (GP) hydrolysate, without enzymatic treatment, as a sole growth medium for BC production by acetic acid bacteria (AAB). The central composite design (CCD) was used to optimise the GP hydrolysate preparation toward the highest reducing sugar contents (10.4 g/L) and minimal phenolic contents (4.8 g/L). The experimental screening of 4 differently prepared hydrolysates and 20 AAB strains identified the recently described species Komagataeibacter melomenusus AV436T as the most efficient BC producer (up to 1.24 g/L dry BC membrane), followed by Komagataeibacter xylinus LMG 1518 (up to 0.98 g/L dry BC membrane). The membranes were synthesized in only 4 days of bacteria culturing, 1 st day with shaking, followed by 3 days of static incubation. The produced BC membranes in GP-hydrolysates showed, in comparison to the membranes made in a complex RAE medium 34 % reduction of crystallinity index with the presence of diverse cellulose allomorphs, presence of GP-related components within the BC network responsible for the increase of hydrophobicity, the reduction of thermal stability and 48.75 %, 13.6 % and 43 % lower tensile strength, tensile modulus, and elongation, respectively. Here presented study is the first report on utilising a GP-hydrolysate without enzymatic treatment as a sole culture medium for efficient BC production by AAB, with recently described species Komagataeibacter melomenusus AV436T as the most efficient producer in this type of food-waste material. The scale-up protocol of the scheme presented here will be needed for the cost-optimisation of BC production at the industrial levels.