Enzymatic soy protein hydrolysis: A tool for biofunctional food ingredient production.
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ABSTRACT:
SUBMITTER: Coscueta ER
PROVIDER: S-EPMC6694868 | biostudies-literature |
REPOSITORIES: biostudies-literature
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Project description:Background:Liquid hot water (LHW) pretreatment has been considered as one of the most industrially viable and environment-friendly methods for facilitating the transformation of lignocelluloses into biofuels through biological conversion. However, lignin fragments in pretreatment hydrolysates are preferential to condense with each other and then deposit back onto cellulose surface under severe conditions. Particularly, lignin tends to relocate or redistribute under high-temperature LHW pretreatment conditions. The lignin residues on the cellulose surface would result in significant nonproductive binding of cellulolytic enzymes, and therefore negatively affect the enzymatic conversion (EC) of glucan in pretreated substrates. Although additives such as bovine serum albumin (BSA) and Tween series have been used to reduce nonproductive binding of enzymes through blocking the lignin, the high cost or non-biocompatibility of these additives limits their potential in industrial applications. Results:Here, we firstly report that a soluble soy protein (SP) extracted from inexpensive defatted soy powder (DSP) showed excellent performance in promoting the EC of glucan in LHW-pretreated lignocellulosic substrates. The addition of the SP (80 mg/g glucan) could readily reduce the cellulase (Celluclast 1.5 L®) loading by 8 times from 96.7 to 12.1 mg protein/g glucan and achieve a glucan EC of 80% at a hydrolysis time of 72 h. With the same cellulase (Celluclast 1.5 L®) loading (24.2 mg protein/g glucan), the ECs of glucan in LHW-pretreated bamboo, eucalyptus, and Masson pine substrates increased from 57%, 54% and 45% (without SP) to 87%, 94% and 86% (with 80 mg SP/g glucan), respectively. Similar effects were also observed when Cellic CTec2, a newer-generation cellulase preparation, was used. Mechanistic studies indicated that the adsorption of soluble SP onto the surface of lignin residues could reduce the nonproductive binding of cellulolytic enzymes to lignin. The cost of the SP required for effective promotion would be equivalent to the cost of 2.9 mg cellulase (Celluclast 1.5 L®) protein (or 1.2 FPU/g glucan), if a proposed semi-simultaneous saccharification and fermentation (semi-SSF) model was used. Conclusions:Near-complete saccharification of glucan in LHW-pretreated lignocellulosic substrates could be achieved with the addition of the inexpensive and biocompatible SP additive extracted from DSP. This simple but remarkably effective technique could readily contribute to improving the economics of the cellulosic biorefinery industry.
| S-EPMC6417190 | biostudies-literature
Project description:Bacterial cellulose nanocrystals (BCNCs) obtained by enzymatic hydrolysis have been loaded in pullulan biopolymer for use as nanoparticles in the generation of high-oxygen barrier coatings intended for food packaging applications. Bacterial cellulose (BC) produced by Komagataeibacter sucrofermentans was hydrolyzed by two different enzymatic treatments, i.e., using endo-1,4-?-glucanases (EGs) from Thermobifida halotolerans and cellulase from Trichoderma reesei. The hydrolytic activity was compared by means of turbidity experiments over a period of 145 h, whereas BCNCs in their final state were compared, in terms of size and morphology, by atomic force microscopy (AFM) and dynamic light scattering (DLS). Though both treatments led to particles of similar size, a greater amount of nano-sized particles (?250 nm) were observed in the system that also included cellulase enzymes. Unexpectedly, transmission electron microscopy (TEM) revealed that cellulose nanoparticles were round-shaped and made of 4-5 short (150-180 nm) piled whiskers. Pullulan/BCNCs nanocomposite coatings allowed an increase in the overall oxygen barrier performance, of more than two and one orders of magnitude (?0.7 mL·m-2·24 h-1), of pure polyethylene terephthalate (PET) (?120 mL·m-2·24 h-1) as well as pullulan/coated PET (?6 mL·m-2·24 h-1), with no significant difference between treatments (hydrolysis mediated by EGs or with the addition of cellulase). BCNCs obtained by enzymatic hydrolysis have the potential to generate high oxygen barrier coatings for the food packaging industry.
| S-EPMC7221805 | biostudies-literature
Project description:BackgroundDuring cellulosic ethanol production, cellulose hydrolysis is achieved by synergistic action of cellulase enzyme complex consisting of multiple enzymes with different mode of actions. Enzymatic hydrolysis of cellulose is one of the bottlenecks in the commercialization of the process due to low hydrolysis rates and high cost of enzymes. A robust hydrolysis model that can predict hydrolysis profile under various scenarios can act as an important forecasting tool to improve the hydrolysis process. However, multiple factors affecting hydrolysis: cellulose structure and complex enzyme-substrate interactions during hydrolysis make it diffucult to develop mathematical kinetic models that can simulate hydrolysis in presence of multiple enzymes with high fidelity. In this study, a comprehensive hydrolysis model based on stochastic molecular modeling approch in which each hydrolysis event is translated into a discrete event is presented. The model captures the structural features of cellulose, enzyme properties (mode of actions, synergism, inhibition), and most importantly dynamic morphological changes in the substrate that directly affect the enzyme-substrate interactions during hydrolysis.ResultsCellulose was modeled as a group of microfibrils consisting of elementary fibrils bundles, where each elementary fibril was represented as a three dimensional matrix of glucose molecules. Hydrolysis of cellulose was simulated based on Monte Carlo simulation technique. Cellulose hydrolysis results predicted by model simulations agree well with the experimental data from literature. Coefficients of determination for model predictions and experimental values were in the range of 0.75 to 0.96 for Avicel hydrolysis by CBH I action. Model was able to simulate the synergistic action of multiple enzymes during hydrolysis. The model simulations captured the important experimental observations: effect of structural properties, enzyme inhibition and enzyme loadings on the hydrolysis and degree of synergism among enzymes.ConclusionsThe model was effective in capturing the dynamic behavior of cellulose hydrolysis during action of individual as well as multiple cellulases. Simulations were in qualitative and quantitative agreement with experimental data. Several experimentally observed phenomena were simulated without the need for any additional assumptions or parameter changes and confirmed the validity of using the stochastic molecular modeling approach to quantitatively and qualitatively describe the cellulose hydrolysis.
| S-EPMC3664589 | biostudies-literature
Project description:Hydrolysis of protein by proteases produces small molecular weights (MWs) peptides as nanomaterials that are easily absorbed. This study investigated the physicochemical properties and antioxidant activity of three plant protein isolates (PIs) including soy, wheat and pea after multi-enzyme hydrolysis. The MWs, particle size and microstructure of PI hydrolysate (PIH) were determined by SDS-PAGE and MALDI-TOF-MS mass spectrometry, dynamic light scattering and transmission electron microscopy, respectively. Cell viability was determined in vitro using a mouse skeletal muscle cell line (C2C12) and crystal violet staining. The MWs and particle sizes of the three plant PIs were reduced after hydrolysis by three proteases (bromelain, Neutrase and Flavourzyme). The MWs of soy, wheat and pea PIH were 103.5-383.0 Da, 103.5-1146.5 Da and 103.1-1937.7 Da, respectively, and particle size distributions of 1.9-2.0 nm, 3.2-5.6 nm and 1.3-3.2 nm, respectively. All three plant PIHs appeared as aggregated nanoparticles. Soy PIH (100 μg/mL) provided better protection against H2O2-induced oxidative damage to C2C12 than wheat or pea PIH. In summary, soy PIH had the best antioxidant activity, and particle size than wheat PIH and pea PIH. Therefore, soy PIH might be a dietary supplement for healthy diet and medical applications.
| S-EPMC8227270 | biostudies-literature
Project description:Non-digestible oligosaccharides (NDOs) are likely prebiotic candidates that have been related to the prevention of intestinal infections and other disorders for both humans and animals. Lignocellulosic biomass is the largest carbon source in the biosphere, therefore cello-oligosacharides (COS), especially cellobiose, are potentially the most widely available choice of NDOs. Production of COS and cellobiose with enzymes offers numerous benefits over acid-catalyzed processes, as it is milder, environmentally friendly and produces fewer by-products. Cellobiohydrolases (CBHs) and a class of endoglucanases (EGs), namely processive EGs, are key enzymes for the production of COS, as they have higher preference toward glycosidic bonds near the end of cellulose chains and are able to release soluble products. In this work, we describe the heterologous expression and characterization of two CBHs from the filamentous fungus Thermothelomyces thermophila, as well as their synergism with proccessive EGs for cellobiose release from organosolv pretreated spruce and birch. The properties, inhibition kinetics and substrate specific activities for each enzyme are described in detail. The results show that a combination of EGs belonging to Glycosyl hydrolase families 5, 6, and 9, with a CBHI and CBHII in appropriate proportions, can enhance the production of COS from forest materials, underpinning the potential of these biocatalysts in the production of NDOs.
| S-EPMC5917092 | biostudies-literature
Project description:The maximum yield of xylanase from Aureobasidium melanogenum PBUAP46 was 5.19?±?0.08 U ml-1 when cultured in a production medium containing 3.89% (w/v) rice straw and 0.75% (w/v) NaNO3 as carbon and nitrogen sources, respectively, for 72 h. This enzyme catalyzed well and was relatively stable at pH 7.0 and room temperature (28?±?2 °C). The produced xylanase was used to hydrolyze xylans from four tropical weeds, whereupon it was found that the highest amounts of reducing sugars in the xylan hydrolysates of cogon grass (Imperata cylindrical), Napier grass (Pennisetum purpureum), and vetiver grass (Vetiveria zizanioides) were at 20.44?±?0.84, 17.50?±?0.29, and 19.44?±?0.40 mg 100 mg xylan-1, respectively, but it was not detectable in water hyacinth (Eichhornia crassipes) hydrolysate. The highest combined amount of xylobiose and xylotriose was obtained from vetiver grass; thus, it was selected for further optimization. After optimization, xylanase digestion of vetiver grass xylan at 27.94 U g xylan-1 for 92 h 19 min gave the highest amount of reducing sugars (23.65?±?1.34 mg 100 mg xylan-1), which were principally xylobiose and xylotriose. The enriched XOs exhibited a prebiotic property, significantly stimulating the growth of Lactobacillus brevis and L. casei by a factor of up to 3.5- and 6.5-fold, respectively, compared to glucose.
| S-EPMC6349264 | biostudies-literature
Project description:Lignocellulosic biomass such as agricultural and forest residues are considered as an alternative, inexpensive, renewable, and abundant source for fuel ethanol production. In the present study, three different pretreatment methods for rice straw were carried out to investigate the maximum lignin removal for subsequent bioethanol fermentation. The chemical pretreatments of rice straw were optimized under different pretreatment severity conditions in the range of 1.79-2.26. Steam explosion of rice straw at 170 °C for 10 min, sequentially treated with 2% (w/v) KOH (SEKOH) in autoclave at 121 °C for 30 min, resulted in 85 ± 2% delignification with minimum sugar loss. Combined pretreatment of steam explosion and KOH at severity factor (SF 3.10) showed improved cellulose fraction of biomass. Furthermore, enzymatic hydrolysis at 30 FPU/g enzyme loading resulted in 664.0 ± 5.39 mg/g sugar yield with 82.60 ± 1.7% saccharification efficiency. Consequently, the hydrolysate of SEKOH with 58.70 ± 1.52 g/L sugars when fermented with Saccharomyces cerevisiae OBC14 showed 26.12 ± 1.24 g/L ethanol, 0.44 g/g ethanol yield with 87.03 ± 1.6% fermentation efficiency.
| S-EPMC5605473 | biostudies-literature
Project description:Bovine cruor, a slaughterhouse waste, was mainly composed of hemoglobin, a protein rich in antibacterial and antioxidant peptides after its hydrolysis. In the current context of food safety, such bioactive peptides derived from enzymatic hydrolysis of hemoglobin represent potential promising preservatives for the food sector. In this work, the hemoglobin hydrolysis to produce bioactive peptides was performed in a regulated pH medium without the use of chemical solvents and by an eco-efficient process: electrodialysis with bipolar membrane (EDBM). Bipolar/monopolar (anionic or cationic) configuration using the H+ and OH- generated by the bipolar membranes to regulate the pH was investigated. The aim of this study was to present and identify the bioactive peptides produced by EDBM in comparison with conventional hydrolysis and to identify their biological activity. The use of the EDBM for the enzymatic hydrolysis of hemoglobin has allowed for the production and identification of 17 bioactive peptides. Hydrolysates obtained by EDBM showed an excellent antimicrobial activity against six strains, antioxidant activity measured by four different tests and for the first time anti-fungal activities against five yeasts and mold strains. Consequently, this enzymatic hydrolysis carried out in regulated pH medium with bipolar membranes could provide bioactive peptides presenting antibacterial, antifungal and antioxidant interest.
| S-EPMC7600257 | biostudies-literature
Project description:Soybean allergy is of great concern and continues to challenge both consumer and food industry. The present study investigates the enzyme-assisted reduction in major soybean allergens in soy protein isolate using different food-grade proteases, while maintaining or improving the sensory attributes and technofunctional properties. SDS-PAGE analyses showed that hydrolysis with Alcalase, Pepsin, and Papain was most effective in the degradation of the major soybean allergens with proteolytic activities of 100%, 100%, and 95.9%, respectively. In the course of hydrolysis, the degree of hydrolysis increased, and Alcalase showed the highest degree of hydrolysis (13%) among the proteases tested. DSC analysis confirmed the degradation of major soybean allergens. The sensory experiments conducted by a panel of 10 panelists considered the overall improved sensory properties as well as the bitterness of the individual hydrolysates. In particular, Flavourzyme and Papain were attractive due to a less pronounced bitter taste and improved sensory profile (smell, taste, mouthfeeling). Technofunctional properties showed a good solubility at pH 7.0 and 4.0, emulsifying capacity up to 760 mL g(-1) (Flavourzyme) as well as improved oil-binding capacities, while the water-binding properties were generally decreased. Increased foaming activity for all proteases up to 3582% (Pepsin) was observed, whereas lower foaming stability and density were found. The hydrolysates could potentially be used as hypoallergenic ingredients in a variety of food products due to their improved technofunctional properties and a pleasant taste.
| S-EPMC4708632 | biostudies-other
Project description:Fish discards are of major concern in new EU policies. Alternatives for the management of the new biomass that has to be landed is compulsory. The production of bioactive compounds from fish protein hydrolysates (FPH) has been explored in recent years. However, the viability of Scyliorhinus canicula discards, which might account for up to 90-100% of captures in mixed trawler, gillnet, and longline industrial fisheries, to produce FPH from the muscle with bioactivities has still not been studied in terms of the optimization of the experimental conditions to enhance its production. The effect of pH and temperature on the hydrolysis of the S.canicula muscle was mediated by three commercial proteases using response surface methodology. Temperatures of 64.6 °C and 60.8 °C and pHs of 9.40 and 8.90 were established as the best hydrolysis conditions for Alcalase and Esperase, respectively. Optimization of the best conditions for the maximization of antihypertensive and antioxidant activities was performed. Higher Angiotensin-converting enzyme (ACE) activity was found with Esperase. The pH optimum and temperature optimum for antioxidants were 55 °C/pH8.0 for ABTS/DPPH-Esperase, 63.1 °C/pH9.0 for DPPH-Alcalase, and 55 °C/pH9.0 for ABTS-Alcalase. No hydrolysis was detected when using Protamex.
| S-EPMC5666414 | biostudies-literature