玉米蛋白复合风味蛋白酶水解物性质的研究

以玉米蛋白为原料,主要研究了通过复合风味蛋白酶水解制备的玉米蛋白水解物的功能特性。结果表明:玉米蛋白经复合风味蛋白酶水解后水解度为11.43%,体外实验该水解度下的玉米蛋白水解物结合胆汁酸的能力较强,相对分子质量分布在10 000～180 Da之间,水解物中有高含量的疏水性氨基酸残留。玉米蛋白水解物持水性为2.95 mL/g,持油性为2.13 mL/g,乳化性为49.96 mL/g,起泡性为126%。玉米蛋白水解物经Sephadex G-15、RP-HPLC分离纯化,对含量最高的组分F2,用MALDI-TOF/TOF MS/MS方法进行鉴定,其相对分子质量为244.2 Da,氨基酸组成为脯氨酸-谷氨酰胺。     

Antioxidant activity,functional properties and bioaccessibility of whey protein hydrolysates

The main objective of this study was to produce the functionally improved whey protein hydrolysate with high bioaccessible antioxidant activity. The hydrolysate with highest antioxidant activity, mainly composed of hydrophilic antioxidant peptides and suitable for preventing oxidation in polar food matrices, was produced by tryptic hydrolysis conducted at 37 °C and an enzyme/substrate (E/S) ratio of 0.5%. The hydrolysate exerted significantly improved antioxidant activity (80.0%), digestibility (95.9%) and bioaccessibility (124.6%) compared to the native whey proteins (32.1%, 87.1% and 106.3%, respectively) as widely used food supplement. The high bioaccessibility indicates the preservation of hydrolysate bioactivity during the process of gastrointestinal digestion, as a particular challenge in its application.     

Whey protein concentrate/λ-carrageenan systems: Effect of processing parameters on the dynamics of gelation and gel properties

The thermal characteristics, dynamics of gelation and gel properties of commercial whey protein concentrate (WPC), WPC/λ-carrageenan (λ-C) mixtures (M) and WPC/λ-C spray-dried mixtures (DM) have been characterized. In a second stage, the effect of the gelling variables (T, pH, total solid content) on gelation and textural properties of DM was evaluated through a Doehlert uniform shell design.The presence of λ-C either in mixtures (M) or in DM promoted the WPC gelation at lower concentration (8%). M showed higher rates of formation and better gel properties (higher hardness, adhesiveness, springiness and cohesiveness) than DM.Nevertheless, when the effects of pH (6.0–7.0), heating temperature (75–90 °C) and total solid content (12–20 wt%) on gelation dynamics and gel properties of DM were studied, gels with a wide range of rheological and textural properties were obtained. While pH did not affect the gelation dynamics, it had some effect on rheological and textural properties. Total solid content and heating temperature were the most important variables for the dynamics of gelation (gelation rate (1/t_gel), gelation temperature (T_gel), rate constant of gel structure development (k_G), elastic modulus after cooling (G′_c) and textural parameters (hardness, springiness and cohesiveness).     

Effect of heat treatment and solution preparation procedure on colloidal stability of whey protein sour cherry beverage

In this study, a whey protein sour cherry beverage was prepared using whey protein concentrate, sour cherry concentrate, Angum gum, water and sugar as initial ingredients. Whey protein concentrate and gum solutions were prepared by four methods. Heat treatment of the solutions led to denaturation of proteins, a change in the solubility of proteins and sediment formation. Our results showed that denaturation of proteins made the peptide fragments of the proteins to bind the gum, thus preventing the separation of the serum.     

Influence of tribomechanical micronization on the physical and functional properties of whey proteins

Because of their high nutritional value and commercially important functional properties, whey proteins are of high interest nowadays. Whey protein concentrates (WPCs) containing 60% and 80% proteins (WPC-60 and WPC-80, respectively) were treated using laboratory equipment for tribomechanical micronization and activation (TMA) with three different rotor speeds: 16 000, 20 000 and 22 000 r.p.m. The results showed that the TMA treatment causes a significant decrease (  P < 0.05) in particle size, a change in particle size distribution and an increase in specific area of WPC. As a consequence of the TMA process, rupturing of protein globules and the appearance of a greater number of protein fragments occurred. The solubility, dispersibility, foaming and emulsifying properties of tribomechanically treated whey protein concentrates (TWPCs) were also modified. The results of particle analysis confirmed that a decrease in particle size correlates with an improvement of the foaming properties. These changes in the treated materials depend on the type of the WPCs used and the rotor speed of the TMA equipment. The most obvious changes were observed in samples treated at the maximum rotor speed of the TMA equipment.     

Developments in whey protein and lactose permeate production processes and their relationship to specific product attributes

This paper reviews recent developments in whey processing and the production of whey protein concentrate and lactose permeate powders with particular reference to a new whey processing facility in the Netherlands. The processes have been designed to optimise product quality with the whey protein concentrate targeted for use in nutritional applications and the permeate powder for use in lactose replacement.     

Functional and bioactive properties of fish protein hydolysates and peptides: A comprehensive review

Global fish processing industries dispose of fish wastes that account for more than 60% of processed fish biomass. In lieu of environmental pollution and disposal problems, these wastes are used to produce fish silage, fishmeal and sauce. They are also utilized for the production of value added products such as proteins, hydrolysates, bioactive peptides, collagen and gelatin. Research on the production of fish protein hydroysates (FPHs) presently focuses on maximizing the industrial potential of fish wastes. Since bioactive peptides containing amino acids hold properties of great interest, this paper reviews current research on the functional and bioactive properties of FPHs with an additional focus on gaps between fish and other hydrolysates, as well as current and future trends for the productive utilization of FPHs.     

Factors Affecting the Functional Properties of Whey Protein Products: A Review

Numerous why protein products (WPP) have been developed as excellent food ingredients with unique functional properties. However, the functional properties of WPP are affected by several compositional and processing factors. Recently, novel processing technologies such as high hydrostatic pressure, ultrasound, extrusion and tribomechanical activation have been used to modify the functional properties of WPP. Also, WPP have been used as delivery systems for functional ingredients and in edible films. The present paper reviews the latest developments in the role of different factors on the functional properties of WPP with emphasis on novel processing technologies, and interaction with other food ingredients     

Functional properties of protein hydrolysates from pea (Pisum sativum,L) seeds

The aim of this study was to investigate the effects of partial enzymatic hydrolysis on functional properties of two different pea protein isolates obtained from two pea genotypes, Maja and L1. Papain and commercial protease (Streptomyces griseus protease) were used for protein modification. Solubility, emulsifying and foaming properties were estimated at four different pH values (3.0, 5.0, 7.0 and 8.0). Papain increased solubility of L1 pea protein isolate at pH 3.0, 5.0 and 8.0, emulsifying properties and foaming capacity at all pH values. Otherwise, papain increased solubility of Maja pea protein isolate only at pH 8.0. This pea protein isolate modified with both enzymes formed emulsions with improved stability at lower pH (3.0, 5.0). The commercial protease‐prepared pea protein isolates showed generally low solubility and different emulsifying and foaming properties. Proper selection of enzyme, conditions of hydrolysis and genotypes could result in production of pea protein isolates with desirable functional properties.     

Simplified process for the production of sesame protein concentrate. Differential scanning calorimetry and nutritional,physicochemical and functional properties

The effects of a simplified production process on the yield, protein content and differential scanning calorimetric analysis of a sesame protein concentrate were studied. The results were compared with those for similar products obtained by the traditional method. The protein content of the (spray‐dried) sesame concentrate obtained by the simplified process (549 g kg^?1) was similar to that of the concentrates obtained by the traditional method (515–565 g kg^?1). Spray‐dried samples showed higher T_d and T_m and lower ΔH than freeze‐dried samples. In addition, the chemical composition, nutritional quality and physicochemical and functional characteristics of the sesame protein concentrate obtained by the simplified process were compared with those of a similar soybean product. The protein, lysine and calcium contents of the sesame concentrate were lower than those of the soybean concentrate, but the digestibility of the protein was the same for both products. The phytic acid content of the sesame concentrate diminished significantly, but was still higher than that of the soybean concentrate. The water absorption and protein solubility were higher for the soybean concentrate, whereas the oil absorption and viscosity at pH 3 were higher for the sesame concentrate. Copyright © 2003 Society of Chemical Industry     

Whey protein concentrate and gum tragacanth as fat replacers in nonfat yogurt: chemical, physical, and microstructural properties

The effect of whey protein concentrate (WPC) and gum tragacanth (GT) as fat replacers on the chemical, physical, and microstructural properties of nonfat yogurt was investigated. The WPC (7.5, 15, and 20 g/L) and GT (0.25, 0.5, 0.75, and 1 g/L) were incorporated into the skim milk slowly at 40 to 45°C with agitation. The yogurt mixes were pasteurized at 90°C for 10 min, inoculated with 0.1% starter culture, and incubated at 42°C to pH 4.6, then refrigerated overnight at 5°C. A control nonfat yogurt and control full fat yogurt were prepared as described, but without addition of WPC and GT. Increasing amount of WPC led to the increase in total solids, total protein, acidity, and ash content, whereas GT did not affect chemical parameters. Increasing WPC caused a more compact structure consisting of robust casein particles and large aggregates. Firmness was increased and susceptibility to syneresis was decreased as WPC increased. No significant difference was observed for firmness and syneresis of yogurt fortified with GT up to 0.5 g/L compared with control nonfat yogurt. Increasing the amount of gum above 0.5 g/L produced softer gels with a greater tendency for syneresis than the ones prepared without it. Addition of GT led to the coarser and more open structure compared with control yogurt.     

Changes in physicochemical and functional properties of whey protein concentrate upon succinylation

The highest degree of succinylation was achieved at the level of 6 moles of succinic anhydride/mole of lysine in whey protein concentrate (WPC). Structural modification of protein or the presence of a high negative charge on the surface of protein upon succinylation exposed buried hydrophobic sites. The solubility of succinylated protein derivatives increased at alkaline pH but decreased at acidic pH values as compared to native WPC. The physicochemical properties of succinylated protein derivatives, such as water– and oil– binding capacity, viscosity and emulsion properties increased significantly (P < 0.05) compared to native WPC, whereas, foaming stability reduced significantly (P < 0.05) and there was no change in the foaming capacity.     

Influence of the degree of hydrolysis on the bioactive properties of whey protein hydrolysates using Alcalase®

Whey protein concentrate was enzymatically hydrolysed at several time courses using the commercial preparation Alcalase^® 2.4 L, different hydrolysates were achieved, and the effect of degree of hydrolysis (DH) on both technological and biological properties was studied. Results have shown that solubility, antioxidant and ACE inhibition activities were increased as DH was also augmented from about 8 to 17%. RP‐HPLC studies also revealed a decrease in hydrophobicity when samples were hydrolysed in comparison with controls. When the enzyme hydrolytic action was augmented, it stimulated both the bioactivity of whey protein and relevant technological properties, allowing these hydrolysates to be employed as additives in the development of food formulations.     

Some functional properties of oat bran protein concentrate modified by trypsin

Oat bran protein concentrate (OBPC) was prepared from oat bran, and hydrolyzed using trypsin. Protein hydrolysates of three different degrees of hydrolysis (4.1%, 6.4% and 8.3% respectively) were obtained. SDS-PAGE analysis demonstrated that oat globulin was the major protein component in OBPC. After trypsin treatment, acidic polypeptides were partly degraded into large peptides (M_r = 29,000–33,000) and small peptides (M_r < 20,000); however, basic polypeptides were almost intact. The functional properties of the resulting products were compared with those of control OBPC. Marked changes in the protein functionality were caused by proteolysis. The solubility, water-holding capacity, emulsifying activity and foaming ability of the hydrolysates gradually increased with the increase in DH. However, the oil-holding capacity, emulsifying stability and foaming stability of the hydrolysates reduced to a certain extent.     

Functional properties of whey protein concentrate texturized at acidic pH: Effect of extrusion temperature

Reactive supercritical fluid extrusion (RSCFX) process at acidic condition (pH 3.0) was used to generate texturized whey protein concentrate (TWPC) and the impacts of process temperature on product's physicochemical properties were evaluated. TWPC extruded at 50 and 70 °C formed soft-textured aggregates with high solubility than that extruded at 90 °C that formed protein aggregates with low solubility. Total free sulfhydryl contents and solubility studies in selected buffers indicated that TWPC is primarily stabilized by non-covalent interactions. Proteins texturized at 90 °C showed an increased affinity for 1-anilino-naphthalene-8-sulfonate (ANS) and a decreased affinity for cis-parinaric acid (CPA), indicating changes in protein structure. Water dispersion of TWPC at room temperature showed thickening function with pseudoplastic behavior. Secondary gelation occurred in TWPC obtained at 50 and 70 °C by heating the cold-set gels to 95 °C. TWPC texturized at 90 °C produced cold-set gels with good thermal stability. Compared to control, TWPC formed stable oil-in-water emulsions. Factors such as degree of protein denaturation and the balance of surface hydrophobicity and solubility influenced the heat- and cold-gelation and emulsifying properties of the protein ingredients. TWPC generated by low and high temperature extrusions can thus be utilized for different products requiring targeted physicochemical functionalities.     

Studies on purification and the molecular mechanism of a novel ACE inhibitory peptide from whey protein hydrolysate

This study sought to purify and identify a novel angiotensin I-converting enzyme (ACE) inhibitory peptide from whey protein hydrolysed by trypsin. The peptide’s amino acid sequence, as well as the molecular mechanism of the interactions between the peptide and the ACE, were also studied. Using ultrafiltration, the hydrolysate was separated into three fractions. The fraction with molecular weight of <6 kDa had the greatest ACE inhibitory activity and was further separated by size exclusion chromatography on Sephadex G-25 and G-10 columns. Reverse-phase high performance liquid chromatography (RP-HPLC) was used to separate the most active fraction. The amino acid sequence of the peptide with the greatest ACE inhibitory characteristics was confirmed as Leu–Leu (LL). The molecular mechanisms, position, type, and energy of the LL/ACE interaction were investigated by using flexible molecule docking technology.     

Fish protein hydrolysates: production, biochemical, and functional properties

Considerable amounts of fish processing byproducts are discarded each year. By developing enzyme technologies for protein recovery and modification, production of a broad spectrum of food ingredients and industrial products may be possible. Hydrolyzed vegetable and milk proteins are widely used food ingredients. There are few hydrolyzed fish protein foods with the exception of East Asian condiments and sauces. This review describes various manufacturing techniques for fish protein hydrolysates using acid, base, endogenous enzymes, and added bacterial or digestive proteases. The chemical and biochemical characteristics of hydrolyzed fish proteins are discussed. In addition, functional properties of fish protein hydrolysates are described, including solubility, water-holding capacity, emulsification, and foam-forming ability. Possible applications of fish protein hydrolysates in food systems are provided, and comparison with other food protein hydrolysates where pertinent.     

Effect of spray drying and freeze drying on the immunomodulatory activity,bitter taste and hygroscopicity of hydrolysate derived from whey protein concentrate

The main aim of the present work was to obtain microencapsulated whey protein concentrate hydrolysate (WPCH) in order to reduce its bitter taste and resistance to hygroscopicity without impairing its immunoregulatory activity by spray drying or freeze drying with whey protein concentrate (WPC) and sodium alginate (SA) as carriers. To attenuate its bitter taste, the WPCH were encapsulated with WPC or the mixture of WPC and sodium alginate (WPC/SA). The splenocyte proliferation activity, hygroscopicity, bitter taste and morphology of non-encapsulated WPCH and encapsulated WPCH were evaluated. Results revealed that WPCH could significantly enhance splenocyte proliferation activity compared with WPC itself. Both spray drying and freeze drying with or without carrier material addition did not exert negative effect on the immunomodulatory activity of WPCH. The bitterness, determined by taste dilution analysis method, of both WPC-encapsulated WPCH and WPC/SA-encapsulated WPCH was significantly lower than that of the original non-encapsulated WPCH. Morphological analysis showed that freeze drying process could not encapsule WPCH as spray drying did. All of these indicated that spray drying with WPC or the mixture of WPC and SA (WPC/SA) as carriers was beneficial for reducing the bitter taste and hygroscopicity without impairing the immunoregulatory activity of whey protein hydrolysate.