The cost of enzymolysis is a major bottleneck for the industrialisation of lignocellulosic enzymatic hydrolysis technology, and recycling cellulase can reduce this cost. Herein, a sulfobetaine prepolymer (CPS) with terminal chlorine was grafted onto enzymatic hydrolysis residual lignin (EHL) from corncob to construct thermosensitive lignin-based \"molecular glues\" (lignin-based sulfobetaine polymers, L-CPS) that were used to recover and recycle cellulase. L-CPS2 (1.0 g/L) was added to the corncob residue (CCR) enzymolysis system (50 °C, pH 4.5). After hydrolysis, L-CPS2 co-precipitated with cellulase through hydrophobic binding when cooling to 25 °C. This co-precipitation decreased the amount of cellulase by 40 %. In summary, a thermally responsive lignin-based molecular glue was constructed for green recycling of cellulase, providing a new approach to decreasing the cost of lignocellulosic enzymolysis and high value utilisation of industrial lignin.

In this experiment, the co-constructed O/W emulsions of different soy protein hydrolysates (SPHs) and gum arabic (GA) were investigated. SPHs were prepared by hydrolyzing soy protein isolate (SPI) using different enzymes, and investigated the effects of enzyme types and hydrolysis time on the physicochemical properties of SPHs. Moreover, SPI/GA and SPHs/GA were prepared and used as hydrophilic emulsifiers to construct O/W emulsions. The results showed that the optimal hydrolysis times for bromelain, pepsin and trypsin were 2 h (BSPH2), 3 h (PSPH3) and 3 h (TSPH3), respectively. Compared with SPI/GA emulsions, SPHs/GA emulsions had smaller particle size, more negative charge, higher interfacial adsorbed protein, and more stable emulsion systems. During the digestion process, SPHs/GA emulsions were effective in realizing the release of bioactives. In conclusion, enzymatic hydrolysis can be an effective modification technique, and SPHs/GA can be used as an effective emulsifier for the emulsion system.

Grape pomace protein isolate was hydrolysed by Alcalase, Flavourzyme and Protease either individually or in combination to produce hydrolysates with antihypertensive and antimicrobial properties. The degree of hydrolysis (DH) ranged between 22 and 52 % for Protease and Flavourzyme, respectively. Among all treatments, hydrolysates prepared using Flavourzyme exhibited the highest angiotensin-converting enzyme inhibitory (ACEi) activity, with an IC50 value of 91 μg/mL. The peptidomics analysis revealed that the peptides identified in Flavourzyme hydrolysate presented molecular features compatible with its bioactivity, like a high density of ACEi sequences per peptide. The hydrolysates were also able to inhibit the growth of Escherichia coli in a range between 9 and 54 % for Alcalase and Alcalase + Flavourzyme, respectively. Peptides in the most active hydrolysate evidenced a high occurrence of proline residues, which is a structural feature of some antimicrobial peptides.

This study aimed at optimizing process protocols for development of low glycemic index (GI) rice flour (LGIRF) by employing enzymatic hydrolysis method using central composite rotatable design (CCRD). LGIRF was evaluated for pasting, farinographic, spectroscopic and microbiological attributes. Independent variables for optimization included concentrations of α-amylase (0.02-0.12 %), glucoamylase (0.02-0.24 %), as well as the incubation temperature (55-80°C). Resistant starch (RS), glycemic index (GI) and glycemic load (GL) were investigated as response variables. The optimum conditions for development of LGIRF with better quality were- α-amylase concentration of 0.040 %, glucoamylase concentration of 0.070 % and an incubation temperature of 60 °C. The results of mineral analysis revealed significantly (p < 0.05) lower levels of boron, potassium, zinc, phosphorus, magnesium, and manganese in LGIRF, while iron and copper were significantly higher. The viscosity profile as evident from pasting profile and farinographic characteristics of LGIRF were significantly (p < 0.05) lower than native rice flour. 1H NMR and 13C NMR spectroscopic studies showed an increase in flexible starch segments and a decrease in amorphous portion of starch LGIRF, along with chemical shift alterations in carbons 1 and 4. Free fatty acids and total plate count were significantly (p < 0.05) higher in LGIRF although was within limits.

The mechanical pulp industry is diversifying through the manufacture of high-value paper products, such as microfibrillated cellulose. However, the development of fibre quality is still energy-intensive. Enzymatic hydrolysis is hypothesized to promote fibre cutting, greater fibrillation, and reduce refining energy costs. Despite potential benefits, there is little understanding of the mechanisms behind fibre development during enzymatic hydrolysis of mechanical pulp. This work investigates how incubation pH and temperature during enzymatic hydrolysis impact the refining of mechanical pulp short fibres. Incubation with endoglucanase at pH 5 and 60 °C increased fibre cutting by approximately 20 %. Fibrillation was negatively affected at this condition, resulting in increased slim fines formation with refining. Incubation at pH 8 and 80 °C promoted >15 % reduction in fibre length, despite such conditions being associated with low enzyme activity. The pH variation modified the sedimentation height of the fibres and the conductivity of suspensions, indicating a change in fibre surface charge. Fibre morphology changes were induced by enzyme hydrolysis conducted at conditions representative of the full range of pH and temperature observed in mechanical pulp mills.

Enzymatic treatment on lignocellulosic biomass has become a trend in preparing nanocellulose (NC), but the process must be optimized to guarantee high production yield and crystallinity. This study offers insights into an innovative protocol using cultivated fungal cellulase and xylanase to improve NC production from raw oil palm leaves (OPL) using five-factor-four-level Taguchi orthogonal design for optimizing parameters, namely substrate and enzyme loading, surfactant concentration, incubation temperature and time. Statistical results revealed the best condition for producing NC (66.06 % crystallinity, 43.59 % yield) required 10 % (w/v) substrate, 1 % (v/v) enzyme, 1.4 % (w/v) Tween-80, with 72-h incubation at 30 °C. Likewise, the highest sugar yield (47.07 %) was obtained using 2.5 % (w/v) substrate, 2.0 % (v/v) enzyme, 2.0 % (w/v) Tween-80, with 72-h incubation at 60 °C. The auxiliary enzymes used in this study, i.e., xylanase, produced higher crystallinity NC, showing widths between 8 and 12 nm and lengths >1 μm and sugars at 47.07 % yield. Thus, our findings proved that optimizing the single-step enzymatic hydrolysis of raw OPL could satisfactorily produce relatively crystalline NC and sugar yield for further transformation into bio-nanocomposites and biofuels. This study presented a simple, innovative protocol for NC synthesis showing characteristics comparable to the traditionally-prepared NC, which is vital for material\'s commercialization.

The application of biopolymer-based materials is increasing due to better sustainability and environmental protection properties. Gelatin fibers have a specific surface and high porosity, which is why their use in medicine and the food industry is being researched. This article explores the potential of centrifugal spinning to produce gelatin fibers. Gelatin for fiber preparation was obtained from a non-traditional source of collagen (chicken by-products) using a unique enzymatic process. The fiber quality was compared with those prepared from gelatins produced from traditional collagen tissues (porcine, bovine). The results showed that fibers cross-linked with glutaraldehyde vapor preserved their structure even in contact with water. Using a cross-linker controlled swelling ability and solubility while maintaining the fiber structure. On the contrary, uncross-linked gelatin fibers were water soluble due to a high surface-to-volume ratio, facilitating water penetration and dissolution. Scanning electron microscopy (SEM) provided a clearer picture of the morphology of gelatin fibers obtained by centrifugal spinning. Differences in the amount of bonding depending on the raw material used and the presence of a cross-linker were analyzed using Fourier transform infrared spectroscopy (FTIR). The overall results showed that chicken gelatin is a suitable alternative to gelatins from traditional sources and can be used for preparing food and pharmaceutical packaging and coatings, fibers, or bioprinting of 3D matrices.

The aim of this research is to propose simple and scalable processes to obtain bioactive peptides extensively hydrolyzed starting from a tuna mixed biomass. The upcycling of this powdered biomass is challenging since it comes from the unsorted industrial side streams of the tuna canning process (cooked residues from fillet trimming) after a patented mild dehydration useful for preventing its degradation until its exploitation. Two different protocols were proposed, with and without the inclusion of an exogenous enzyme (Enzymatic-Assisted Extraction, EAE), with no relevant differences in yields (24% vs. 22%) and a comparable amino acid composition. Nevertheless, the former protocol (with EAE) provided peptides with an average molecular weight of 1.3 kDa, and the second one (without EAE) provided peptides with an average molecular weight of 2.2 kDa. The two corresponding types of tuna protein hydrolysates (Enzymatic Hydrolysates (EH) and Non-Enzymatic Hydrolysates (NEH)) were characterized by proximate compositions, pH, color profile, amino acid analysis, FTIR spectra, and molecular weight distribution. In addition, several biological analyses were performed to assess their potential use as nutraceutical supplements: special attention has been paid to antioxidant activity using three different methods to quantify it. EH showed the most promising antioxidant activity which could be exploited also in other fields (e.g., biomaterials, cosmetics).

This study aimed to rapidly develop novel umami peptides using yeast protein as an alternative protein source. Yeast protein hydrolysates exhibiting pronounced umami intensity were produced using flavorzyme under optimum conditions determined via a sensory-guided response surface methodology. Six out of 2138 peptides predicted to possess umami taste by composite machine learning and assessed as nontoxic, nonallergenic, water-soluble, and stable using integrated bioinformatics were screened as potential umami peptides. Sensory evaluation results revealed these peptides exhibited multiple taste attributes (detection threshold: 0.37 ± 0.10-1.1 ± 0.30 mmol/L), including umami. In light of the molecular docking outcomes, it is inferred that hydrogen bond, hydrophobic, and electrostatic interactions enhanced the theoretically stable binding of peptides to T1R1/T1R3, with their contributions gradually diminishing. Hydrophilic amino acids within T1R1/T1R3, especially Ser, may play a particularly pivotal role in binding with umami peptides. Future research will involve establishing heterologous cell models expressing T1R1 and T1R3 to delve into the cellular physiology of umami peptides. Peptide sequences (FADL, LPDP, and LDIGGDF) also had synergistic saltiness-enhancing effects; to overcome the limitation of not investigating the saltiness enhancement mechanism, comprehensive experiments at the molecular and cellular levels will also be conducted. This study offers a rapid umami peptide development framework and lays the groundwork for exploring yeast protein taste compounds.

The degummed wastewater from silk processing contains a huge amount of amino acids and polypeptides from sericin. The silk degumming water is far from being exploited fully. Sericin in the degumming water is generally wasted and causes environmental pollution. In this study, simulated silk degumming water was hydrolyzed by alkaline protease to produce abundant amino acids and polypeptides. After enzymatic hydrolysis, the maximum free amino groups concentration in the silk degumming water was approximately 54 mM. It facilitated the recycling of silk degumming water for the production of melanin-like amino acid surfactants as raw materials. 4-Tert-butylcatechol was used as the starting material to generate o-quinone via oxidation by ceric ammonium nitrate. o-Quinone was coupled with free amino groups in enzymatic hydrolysates of silk degumming water to synthesize a sericin-based amino acid surfactant as hydrophobic and hydrophilic group, respectively. Through the green and simple synthesis route, the product was characterized to have a novel melanin-like structure. The product exhibited superior surface-active properties by lowering the surface tension to 32.39 mN m-1. Furthermore, it demonstrated good foaming ability and foam stability, with the initial foam volume of 37 mL and the foam half-life time of more than 25 min. The product owned a good emulsification ability in the oil-water emulsion with delamination time of 297 s and 291 s for emulsion formed by soybean oil and liquid paraffin, respectively. The wetting time of the canvas sheet was only 134 s. Consequently, the product showed low surface tension, good foaming, emulsifying, and wetting properties.