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1.
Plant Foods Hum Nutr ; 79(2): 322-329, 2024 Jun.
Article in English | MEDLINE | ID: mdl-38753215

ABSTRACT

This study introduces the concept of developing a functional hemp drink enriched with γ-Aminobutyric acid (GABA) to enhance its nutritional value and functional properties utilizing Solid-State (SSF) co-Fermentation by Lactobacillus casei and Bacillus subtilis and germination bioprocesses. Bioprocesses may offer an alternative solution to challenges in hemp milk, such as product instability and the use of additives. Notably, the hemp milk produced through the germination for three days or co-fermentation processes yielded the highest GABA content of 79.84 and 102.45 mg/100 mL, respectively, compared to the untreated milk. These bioactive milk samples exhibited higher zeta potential and soluble protein content and also reduced solid particle sedimentation and droplet sizes (D4,3 and D3,2) compared to the untreated milk. Furthermore, the peptide, total phenolic content, and antioxidant activity of the produced GABA-enriched kinds of milk surpassed those of the untreated milk. Overall, the SSF and germination processes present a promising alternative for producing stable milk analogs with enhanced health-boosting properties.


Subject(s)
Antioxidants , Bacillus subtilis , Cannabis , Fermentation , Germination , gamma-Aminobutyric Acid , gamma-Aminobutyric Acid/analysis , gamma-Aminobutyric Acid/metabolism , Cannabis/chemistry , Cannabis/growth & development , Antioxidants/analysis , Nutritive Value , Lacticaseibacillus casei/metabolism , Lacticaseibacillus casei/growth & development , Phenols/analysis , Milk/chemistry , Peptides/analysis , Food, Fortified/analysis
2.
Compr Rev Food Sci Food Saf ; 23(3): e13372, 2024 May.
Article in English | MEDLINE | ID: mdl-38795380

ABSTRACT

The burgeoning demand for protein, exacerbated by population growth and recent disruptions in the food supply chain, has prompted a rapid exploration of sustainable protein alternatives. Among these alternatives, algae stand out for their environmental benefits, rapid growth, and rich protein content. However, the widespread adoption of algae-derived proteins faces significant challenges. These include issues related to harvesting, safety, scalability, high cost, standardization, commercialization, and regulatory hurdles. Particularly daunting is the efficient extraction of algal proteins, as their resilient cell walls contain approximately 70% of the protein content, with conventional methods accessing only a fraction of this. Overcoming this challenge necessitates the development of cost-effective, scalable, and environmentally friendly cell disruption techniques capable of breaking down these rigid cell walls, often laden with viscous polysaccharides. Various approaches, including physical, chemical, and enzymatic methods, offer potential solutions, albeit with varying efficacy depending on the specific algal strain and energy transfer efficiency. Moreover, there remains a pressing need for further research to elucidate the functional, technological, and bioaccessible properties of algal proteins and peptides, along with exploring their diverse commercial applications. Despite these obstacles, algae hold considerable promise as a sustainable protein source, offering a pathway to meet the escalating nutritional demands of a growing global population. This review highlights the nutritional, technological, and functional aspects of algal proteins and peptides while underscoring the challenges hindering their widespread adoption. It emphasizes the critical importance of establishing a sustainable trajectory for food production, with algae playing a pivotal role in this endeavor.


Subject(s)
Algal Proteins , Peptides , Peptides/chemistry , Algal Proteins/chemistry
3.
Food Chem ; 442: 138488, 2024 Jun 01.
Article in English | MEDLINE | ID: mdl-38244438

ABSTRACT

The Maillard conjugation of hemp protein with d-xylose was studied, focusing on the influence of ultrasonic waves, processing time, and pressure. Cavitation-driven processes, including ultrasonication (US) and manothermosonication (MTS), were found to impact the degree of grafting, functional characteristics, and structural alterations, affecting conjugation efficiency. The glycation of hemp protein with xylose assisted with US and MTS was investigated under varying pressures. MTS- and US-assisted glycation processes result in 4.22- and 1.64-fold higher degrees of grafting compared to the classical method within a short time frame. The MTS procedures also improved solubility (+3.6-fold), emulsion (+15-fold), and foaming (+1.7-fold) properties, especially at optimized pressure levels, compared to classical conjugates. Furthermore, the complexation of MTS-assisted conjugates with curcumin (Cur) enhanced Cur stability by more than 1.4-fold compared to the classical procedure during 20-day storage at 4 oC. The findings suggest potential applications in the pharmaceutical industry, active dairy/meat analog development, and gel formulation.


Subject(s)
Curcumin , Curcumin/chemistry , Plant Proteins , Chemical Phenomena , Solubility , Emulsions/chemistry , Maillard Reaction
4.
Food Chem ; 439: 138137, 2024 May 01.
Article in English | MEDLINE | ID: mdl-38061300

ABSTRACT

The challenge of preserving the quality of thermal-sensitive polymeric materials specifically proteins during a thermal drying process has been a subject of ongoing concern. To address this issue, we investigated the use of ultrasound contact drying (USD) under non-thermal conditions to produce functionalized pea protein powders. The study extensively examined functional and physicochemical properties of pea protein isolate (PPI) in powder forms obtained through three drying methods: USD (30 °C), spray drying (SD), and freeze drying (FD). Additionally, physical attributes such as powder flowability and color, along with morphological properties, were thoroughly studied. The results indicated that the innovative USD method produced powders of comparable quality to FD and significantly outperformed SD. Notably, the USD-PPI exhibited higher solubility across all pH levels compared to both FD-PPI and SD-PPI. Moreover, the USD-PPI samples demonstrated improved emulsifying and foaming properties, a higher percentage of random coil form (56.2 %), increased gel strength, and the highest bulk and tapped densities. Furthermore, the USD-PPI displayed a unique surface morphology with visible porosity and lumpiness. Overall, this study confirms the effectiveness of non-thermal ultrasound contact drying technology in producing superior functionalized plant protein powders, showing its potential in the fields of chemistry and sustainable materials processing.


Subject(s)
Pea Proteins , Powders/chemistry , Ultrasonics , Freeze Drying/methods , Desiccation/methods
5.
Int J Biol Macromol ; 253(Pt 7): 127240, 2023 Dec 31.
Article in English | MEDLINE | ID: mdl-37806421

ABSTRACT

With the global population on the rise, challenges in meeting protein demands are amplified by recent crises, prompting a swift shift to alternative protein sources due to disruptions in the supply chain. Plant-based proteins are gaining momentum due to economic, cultural, and environmental considerations, aligning with the preference for sustainable diets and resulting in more affordable plant-based products. The distinction between drug and industrial hemp fuels demand for its nutritional value, digestibility, low allergenicity, and bioactive properties. Industrial hempseed, featuring minimal Δ9-Tetrahydrocannabinol (THC) content (<0.2 %), emerges as a promising crop, offering high-quality protein and oil. The de-oiled hempseed cake stands as an eco-friendly and promising protein source enriched with phenolic compounds and fiber. Ongoing research seeks to enhance techno-functional properties of hempseed protein, surmounting initial limitations for integration into various foods. A range of techniques, both conventional and innovative, optimize protein characteristics, while modifying plant-based protein structures augments their application potential. Modification approaches like ultrasound, high-pressure homogenization, conjugation, complexation, fibrillization, and enzymatic methods enhance hempseed protein functionality. The review critically evaluates the techno-functional attributes of hempseed protein and explores strategies for customization through structural modifications. Lastly, the review assesses its composition, potential as a plant-based source, addresses challenges, and discusses strategies for enhanced functionality.


Subject(s)
Cannabis , Seeds , Seeds/chemistry , Cannabis/chemistry , Dronabinol , Diet , Plant Proteins/analysis
6.
Int J Biol Macromol ; 253(Pt 2): 126816, 2023 Dec 31.
Article in English | MEDLINE | ID: mdl-37690656

ABSTRACT

Pea protein isolate (PPI) is a popular plant-based ingredient, typically produced through alkaline-isoelectric precipitation and thermal drying. However, high temperatures and long drying times encountered in thermal drying can denature PPI and cause loss of functionality. This study investigated the use of an innovative ultrasonic dryer (US-D) at 30 °C for drying PPI suspensions, compared to conventional hot air drying (HA-D) at 60 °C. US-D led to an increase in the drying rate and correspondingly reduced the drying time by 55 %, when compared to HA-D. The average effective moisture diffusivity in the US-D process was 325 % higher than that in the HA-D process. The resulting PPI exhibited higher solubility, emulsification, and foaming properties than HA-D PPI, with a unique surface morphology and higher surface area. This study demonstrated that drying with acoustic energy is a promising approach for producing dried plant protein ingredients with improved functional properties, reduced processing time, and increased production efficiency.


Subject(s)
Pea Proteins , Pea Proteins/chemistry , Ultrasonics , Desiccation/methods , Plant Proteins/chemistry , Solubility
7.
Plant Foods Hum Nutr ; 77(4): 577-583, 2022 Dec.
Article in English | MEDLINE | ID: mdl-36227525

ABSTRACT

Ultrasound is one of the non-thermal, green, and novel technologies used to functionalize plant proteins. We recently determined the optimum conditions of high-intensity ultrasound (HIUS) treatment for maximum solubility and investigated the functional properties of hemp seed protein isolate (HSPI) under the optimal conditions. In this study, we analyzed changes in primary, secondary, and tertiary structures, physical microstructures, thermal stability, and antioxidant capacity of ultrasound-applied hemp protein isolate (HSPI-HIUS). The free SH group content (+59%) and zeta potential (+25%) increased upon ultrasound treatment. The electrophoretic protein patterns of HSPI showed no significant change after HIUS treatment. The FTIR spectrum revealed the wavenumber shifts in Amid 1 and 2 regions of protein. The denaturation temperature and the ratio of ß-structure increased after sonication. Antioxidant properties of hemp seed protein isolates were increased by 38% by ultrasound treatment. The obtained data in this study showed that HIUS treatment would be promising for improving the functional, physicochemical, and antioxidant properties of HSPI.


Subject(s)
Antioxidants , Cannabis , Antioxidants/pharmacology , Antioxidants/analysis , Particle Size , Plant Proteins/analysis , Seeds/chemistry
8.
Food Chem ; 375: 131843, 2022 May 01.
Article in English | MEDLINE | ID: mdl-34920309

ABSTRACT

High-intensity ultrasound (HIUS) is one of the physical methods to modify protein functionality. This study aims to improve the functional properties of hemp seed protein isolate (HSPI) based on the solubility and particle size using the Response Surface Methodology. The acoustic intensity of 37 W/cm2 and protein concentration of 6.9% for 7.8 min were optimum process conditions that increased HSPI solubility (78%). The functional properties of ultrasound treated isolate (HSPI-HIUS) under the optimal conditions were compared with untreated HSPI. The results revealed that the emulsification, oil absorption, and foaming properties of HSPI-HIUS significantly enhanced after HIUS, whereas gelling concentration significantly decreased. Enhanced functional properties in HSPI-HIUS have been associated with structural changes based on surface hydrophobicity, particle size, and fluorescence intensity. This study indicated that HIUS can increase the functionality and prevalence of hemp seed protein isolate in food products.


Subject(s)
Cannabis , Chemical Phenomena , Hydrophobic and Hydrophilic Interactions , Particle Size , Solubility
9.
J Food Sci ; 83(3): 763-769, 2018 Mar.
Article in English | MEDLINE | ID: mdl-29437226

ABSTRACT

The molding of food products causing health risks is a main problem in the food industry. In this study, as an alternative solution for preventing mold growth, an antifungal edible film was developed by incorporating Williopsis saturnus var. saturnus (0; 3; 7; and 9 logs CFU/cm2 ) into whey protein concentrate (WPC) based films. Antifungal properties of the films against Penicilium expansum and Aspergillus niger were analyzed using the disc diffusion method. Physical (barrier, solubility, color), mechanical (tensile strength and percent elongation) properties of the films as well as the survival of W. saturnus in the film were assessed during 28 days of storage at 23 °C. According to the results, the viability of W. saturnus (7 and 9 logs CFU/cm2 ) in WPC films stored for 28 days under vacuum or non-vacuum decreased to 36% and 60%, respectively. In addition, films containing W. saturnus decreased the viability of P. expansum and A. niger by 29% and 19%, respectively. Adding yeast did not change the tensile strength (P > 0.05), but significantly decreased % elongation and increased water vapor and oxygen permeability and water solubility (P < 0.05). In conclusion, this study showed that the developed films may be useful for inhibiting mold growth on foods.


Subject(s)
Biofilms , Food Packaging , Food Technology , Williopsis , Antifungal Agents/pharmacology , Aspergillus niger/drug effects , Chemical Phenomena , Hydrogen-Ion Concentration , Microbial Viability , Penicillium/drug effects , Whey Proteins/chemistry
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