Physicochemical,rheological, and molecular characterization of colloidal gelatin produced from Common carp by‐products using microwave and ultrasound‐assisted extraction

The effects of ultrasound‐assisted extraction (UAE) and microwave‐assisted extraction (MAE) methods on molecular and physicochemical characteristics of the resultant gelatin were examined. Before extraction procedure, we investigated the optimum pH for swelling of Common carp by‐products, which is an important pretreatment for gelatin production. The highest swelling yield was achieved at pH 13 among pH 1–14 with unit intervals. Results indicated that the UAE gelatin has a higher gel strength, viscosity, melting point, and gelling point. The power and time of sonication showed a reverse relation with these characteristics. In addition, as the time of microwave heating was raised, the gel strength, viscosity, melting point, and gelling point were decreased. The FT‐IR spectra showed similar peaks but the Amide B in UAE gelatin slightly vanished. The electrophoretic pattern also revealed the higher gel strength and viscosity of UAE gelatin due to the higher intensity of α and β chains compared to MAE gelatin. It can be concluded from all of the results of this study that the produced gelatin using these procedures can be a good source of gelatin in food and drug industries.     

Effects of Alkaline and Acid Pretreatments on Alaska Pollock Skin Gelatin Extraction

Pretreatments with different alkalis and acids at different concentrations were used to determine their effects on gelatin extraction from Alaska pollock skin. The alkaline pretreatments with the OH concentrations lower than 0.5 mol/L removed noncollagenous proteins without significant loss of skin collagen. The acid pretreatments caused loss of collagen, even using a weak acid with a low H concentration at a low temperature. The presence of proteases might cause degradation of gelatin extract, but the pretreatments with NaOH or Ca(OH)₂ at 0.1 mol/L OH concentration, or acetic acid at 0.05 mol/L H concentration could significantly decrease the degradation by proteases. The combination of an alkaline pretreatment followed by an acid pretreatment not only removed the noncollagenous proteins, but also provided the proper pH condition for extraction, during which some cross‐linkages could be further destroyed but with less breakage of polypeptide chains.     

马铃薯凝胶淀粉的理化特性研究

通过与玉米淀粉和马铃薯淀粉相比较,系统研究了马铃薯凝胶淀粉的理化特性,包括:粘度的测定;热糊与冷糊的稳定性;不同pH值及电解质(NaCl)和非电解质(蔗糖)存在下的粘度曲线;凝胶强度;冻融稳定性. 结果表明:马铃薯凝胶淀粉比天然淀粉具有优良的热糊与冷糊的稳定性,电解质(NaCl)和非电解质(蔗糖)的存在,对马铃薯凝胶淀粉的热糊与冷糊的稳定性基本上无影响,凝胶强度高,冻融稳定性好,尤其是耐酸性能强,可作为凝胶剂而广泛应用于各种食品加工体系。     

Rheology of whey protein isolate-xanthan mixed solutions and gels. Effect of pH and xanthan concentration

Flow properties at pH 5.5-7.5 of whey protein isolate (WPI)-xanthan solutions containing 0-0.5 w/w% xanthan were studied by viscosimetry, although rigidity and fracture properties of the corresponding heat-set gels (90°C, 30 min) were determined by uniaxial compression. All the studied solutions displayed generalized shearthinning flow behaviour. Synergistic WPI-xanthan interactions has been revealed by observing that rheological parameters [σ_msf, K, n, η (γ)] characterizing blends were larger than those calculated from the two separated solutions. Such a behaviour was attributed to segregative phase separation of whey proteins and xanthan. Effects of xanthan on WPI-xanthan gel properties both depended on pH and xanthan concentration. Simultaneous increased xanthan concentration and decreased pH inhibited gelation of WPI-xanthan blends. Regarding gel strength, synergistic WPI-xanthan interactions were observed at pH >7.0 and low xanthan concentration (0.05 or 0.1 w/w%). Antagonism between the two macromolecules occurred at low xanthan concentration and pH ≤6.5, and high xanthan concentration (0.2 or 0.5 w/w%) at all pH tested. Low xanthan concentration rendered mixed gels more brittle than protein gels, and high xanthan concentration decreased pH effects on gel stress-strain relationships. The balance between strong thermal aggregation of concentrated whey proteins - in presence of incompatible xanthan -, high viscosity of blends and repulsive surface forces of protein molecules was thought to be at the origin of WPI-xanthan gel mechanical properties.     

The Effects of Acetic Acid Concentration and Extraction Temperature on Physical and Chemical Properties of Pigskin Gelatin

This research was aimed to study the influence of acetic acid concentration and extraction temperature on physical and chemical properties of pigskin gelatin. The experiment used Completely Randomized Design (CRD) with two factors and three replicates of treatment. The first factor was concentration of acetic acid solution consisted of 3 levels (2, 4 and 6%). The second factor was extraction temperature consisted of 3 levels (50, 55 and 60 ^oC). The result showed that interaction of acetic acid and extraction temperature had no significant effect (P>0.05) on the gel strength, viscocity, protein content and pH value of pigskin gelatin. Pigskin gelatin with acetic acid concentration 2, 4 and 6% and extraction temperature up to 60^oC had similar characteristics to the commercial gelatin. The optimum production was obtained from 4% acetic acid and temperature 55^oC such as gel strength 134.22 g/Bloom; viscocity.7.16 cP; protein content 88.56% and pH value 5.21.     

茶叶籽粕蛋白功能特性研究

以大豆分离蛋白为对照,研究碱法和酶法提取茶叶籽粕蛋白的功能特性。结果表明：酶法提取茶叶籽粕蛋白的溶解性、吸油性、乳化能力和乳化稳定性、起泡性、凝胶脆度优于碱法提取茶叶籽粕蛋白,而后者的吸水性、泡沫稳定性则优于前者,两者所形成蛋白凝胶的黏性和硬度相当。碱法和酶法提取的茶叶籽粕蛋白的乳化能力和乳化稳定性稍优于大豆分离蛋白,但起泡性和泡沫稳定性则不及大豆分离蛋白,溶解性与大豆分离蛋白相当,它们形成凝胶的最低质量分数分别为13%和15%,凝胶的黏性和硬度低于大豆分离蛋白。pH值、蛋白质量分数、NaCl浓度等因素对茶叶籽粕蛋白功能特性均有不同程度的影响。     

Digestive acid protease from zebra blenny (Salaria basilisca): Characteristics and application in gelatin extraction

The present study reports on the characterization and evaluation of a crude acidic protease from the viscera of zebra blenny (Salaria basilisca) for use in gelatin extraction. Using hemoglobin, zymogram analysis revealed the presence of at least one clear band. The crude acid protease was noted to be optimally active at pH 3.0 and 50 °C and highly stable over a pH range of 2.0 to 7.0. The enzymatic extract lost about 87% of its activity after incubation with pepstatin A for 30 min at 4 °C. The acidic protease from the viscera of zebra blenny was noted to be effective in the extraction of gelatin from the skin of zebra blenny, with an extraction yield of 14.65% based on the wet weight of zebra blenny skin. The extracted zebra blenny skin gelatin (ZBSG) was characterized based on its chemical composition, polypeptide pattern, gel strength, textural parameters, and functional properties. ZBSG had high protein (90.6%) and low ash (3.1%) and fat (0.6%) contents. It contained α₁ and α₂-chains as the major constituents and determined as belonging to type I. The bloom strength of solidified gelatin was 151.3 g. The findings from Fourier Transformed Infrared (FT-IR) spectroscopy suggested the presence of helical arrangements of ZBSG. The latter showed excellent concentration-dependent functional properties. While emulsion activity index (EAI) and emulsion stability index (ESI) decreased, foam expansion (FE) and foam stability (FS) increased as the concentration of gelatin increased. Overall, zebra blenny endogenous acid protease could open new promising opportunities for the extraction of gelatin.     

Characterization of tilapia (Oreochromis niloticus) skin gelatin extracted with alkaline and different acid pretreatments

Tilapia production is growing worldwide and to better utilize wastes from the processing industry, one important application is production of high quality fish gelatin to meet the needs of markets that are not amenable to beef or porcine gelatin. The extraction process from tilapia skin gelatin was optimized through the use of a combination of alkali (0.3 M NaOH) with different types and concentrations of acids before thermal hydrolysis. The effects of acid pretreatments on the protein yields and the physicochemical properties of tilapia gelatin were investigated. Acid concentrations (0.01–0.20 M) influenced gelatin protein recovery: 10.52%–22.40% for citric acid, 1.92%–21.55% for acetic acid, and 4.47%–24.35% for HCl. It was possible to increase gelatin yield for each of the tested acids by adjusting the acid concentration. Gelatin viscosity and the molecular weight distribution of gelatin proteins were related to the acid concentration used. Gelatin prepared using too low a concentration (e.g. 0.01 M acetic acid or HCl) or too high a concentration (e.g. >0.05 M HCl or citric acid) yielded an extract with a smaller ratio of large molecule components, such as β-chains, and exhibited lower viscosity. The film forming properties of gelatins extracted from three acid-optimized pretreatments showed no significant difference in transparency, tensile strength and elongation at break; though the gelatin film made from 0.03 M citric acid pretreated gelatin had somewhat better water barrier property than those made with HCl or acetic acid.     

影响结冷胶水溶液流变特性的因素

研究了质量分数、时间、温度、柠檬酸、pH值、Na^＋、Ca^2＋对结冷胶水溶液的粘度及形成凝胶后的凝胶强度的影响.结果表明：结冷胶的粘度随着溶液质量分数的增加呈非线性增大,室温下其粘度的稳定时间大于4 h.温度、pH值、柠檬酸对结冷胶水溶液粘度有相应的影响;柠檬酸、NaCl、CaCl2溶液对结冷胶的凝胶强度有较大影响.     

Enhancement of Functional Properties of Wami Tilapia (Oreochromis urolepis hornorum) Skin Gelatin at Different pH Values

The effects of several agents in two different concentrations and pH values (5.0 and 8.0) on the functional properties of tilapia (Oreochromis urolepis hornorum) skin gelatin were evaluated and compared using a control tilapia skin gelatin and a commercial mammalian gelatin. The addition of the agents (sucrose 4 % and 8 % (w/v), glycerol 5 % and 10 % (v/v), NaCl 0.3 and 0.8 mol/L, MgCl₂ 0.3 and 0.8 mol/L, MgSO₄ 0.3 and 0.8 mol/L, KCl 0.3 and 0.8 mol/L, and transglutaminase 10 and 15 mg/mL) slightly increased the turbidity. There were different ratios of rheological properties depending on the agent, concentration, and pH. The addition of all agents increased the viscosity of the gelatin solution, mainly at pH 5.0. The addition of glycerol (10 % (v/v)) raised viscosity up to 7.45 cP. The setting time was prolonged by incorporating the agents. The gelatin samples with the addition of MgSO4 0.8 mol/L showed higher gel strength than the mammalian gelatin, exhibiting values of 298 and 295g_f at pH 5.0 and 8.0, respectively.     

酸/碱预处理对美洲鳗鲡（Anguilla rostrata）鱼骨明胶理化性质与凝胶特性的影响

以美洲鳗鲡（Anguilla rostrata）鱼骨为原料,采用酸或碱预处理结合热水浸提制备鱼骨明胶,并通过得率、凝胶强度测定、SDS-PAGE、紫外全波长扫描、红外光谱扫描、动态流变学测定以及扫描电镜等研究鱼骨明胶的理化性质和凝胶特性。结果表明:酸法预处理明胶（AG60）与碱法预处理明胶（BG60）得率分别为13.6%和6.88%,凝胶强度分别为101.95 g和78.74 g。AG60和BG60的羟脯氨酸含量为3.2 g/100 g和2.7 g/100 g。两种明胶均含有β和α₁、α₂链,其中AG60的α₁+α₂含量显著高于BG60。AG60与BG60均具有明胶的特征吸收峰,且无杂蛋白吸收峰。与BG60相比,AG60具有更高的凝胶温度与熔融温度,以及更短的胶凝时间。扫描电镜分析显示,AG60具有更致密、均一的凝胶网络结构。本研究表明,与碱法预处理相比,酸法预处理制备得到的鳗鱼骨明胶具有更高的得率与更好的凝胶特性。     

Strength of Protein Gels Prepared with Microbial Transglutaminase as Related to Reaction Conditions

Influence of gelling reaction conditions on the strength of several protein gels prepared with microbial transglutaminase (TGase) was investigated. A method was developed to gel proteins and measure gel breaking strength in a micro well plate. Enzyme concentration range for maximum gel breaking strength varied from 10 to 40 units/g protein. Maxima gel breaking strengths were achieved at 50°C for SPI, caseinate and gelatin and 65°C for egg yolk and egg white proteins. Optimum pH resulting in strong gels was pH 9 for SPI, caseinate, and egg yolk, and pH 6 for gelatin and egg white. Adjusting pH was promoted in egg white the formation of ?-(γ-glutamyl)lysine crosslinks and increased its gel breaking strength.     

Characteristics and functional properties of gelatin from zebra blenny (Salaria basilisca) skin

Gelatin was extracted from alkali-pretreated skin of zebra blenny (Salaria basilisca) using commercial pepsin with a yield of 18 g/100 g of skin sample. The polypeptides pattern, gel strength, viscosity, textural parameters and functional properties of the zebra blenny skin gelatin (ZBSG) were investigated. Amino acid analysis revealed that ZBSG contained almost all essential amino acids, with glycine being the most predominant one. ZBSG was identified as a type I gelatin, containing α₁ and α₂-chains as the major constituents. Its gel strength and viscosity were 170.2 g and 5.95 cP, respectively. Fourier transformed infrared spectroscopy (FT-IR) spectra showed helical arrangements in its structure. Its solubility and functional properties were concentration-dependent. While foam expansion (FE) and foam stability (FS) increased with the increase of concentration, emulsifying activity index (EAI) and emulsion stability index (ESI) were noted to decrease. ZBSG also showed strong clarification ability particularly for apple juice, without affecting nutritional value.     

Effects of Pretreatment on Properties of Gelatin from Perch (Lates Niloticus) Skin

Fish gelatins obtained from perch fish skin pretreated with various solutions containing acetic acid, sodium hydroxide (NaOH) and sodium chloride (NaCl) were successfully characterized for their nanostructure pattern using field emission scanning electron microscopy. Each pretreatment transformed collagen to gelatin with fibril, zigzag cracks, straight rods, and cross-linked rods nanostructure patterns. Pretreatment solutions also affect the gel yield, gel strength, amino acid profile, and functional groups in perch gelatin as analyzed by Fourier transform infrared spectroscopy. Samples pretreated with NaCl, NaOH, and acetic acid solution showed the highest gel yield (22.84%) and gel strength (179.84 g). Fourier transform infrared spectra for perch gelatins also revealed weak C–N amide II and III bond stretches as well as weak C=O bond stretch.     

The role of salt washing of fish skins in chemical and rheological properties of gelatin extracted

Dover sole (Solea vulgaris) skins were washed with different salt solutions previous to gelatin extraction by a mild acid pre-treatment. The effects of NaCl, KCl, MgCl₂, MgSO₄ and no-salt washing on the mineral content, yield of extraction, molecular weight distribution, gel strength, aggregation phenomena and viscoelastic properties of gelatin newly dissolved and after overnight cold maturation were evaluated. Skin washing with NaCl and KCl induced noticeable changes in molecular weight distribution, and consequently in gel strength and rheological properties, especially when compared with unsalted gelatin preparations. However, salts containing Mg²⁺ gave rise to the retaining of this bivalent cation in the resultant gelatin, which is detrimental to the gelatin quality.     

Treatment of enzymatic wool with Fe3O4 nanoparticles and citric acid to enhance mechanical properties using RSM

In this work, protease enzymatic wool was treated with citric acid and Fe₃O₄ nanoparticles to produce fabric with enhanced tensile strength, elongation, alkali resistance with controllable hydrophilicity/hydrophobicity through a simple ‘impregnating’ method. Protease enzymatic is also one of the most important processes usually carried out in alkali condition to obtain the desirable characteristics, which enhanced the surface activity and nanoparticles adsorption. Mechanical properties such as tensile strength and elongation were reduced as a consequence of alkali enzymatic pretreatment. Here, with the help of citric acid cross-linking agent, Fe₃O₄ nanoparticles were stabilized on the enzymatic wool surface in a way to revenge reduction in the tensile strength, elongation, alkali resistance. In order to create optimum tensile strength, elongation, alkali resistance, lightness and hydrophilicity/hydrophobicity, the appropriate models were obtained based on Design-Expert software. Overall, the results confirmed that the enzymatic wool fabrics could be modified by citric acid and Fe₃O₄ nanoparticles post-treatment. The Fe₃O₄ nanoparticle/citric acid treatment on the protease enzymatic wool improved tensile strength and elongation along with the higher alkali resistance and controllable hydrophilicity/hydrophobicity.     

Naturally crosslinked gelatin gels with modified material properties

Natural crosslinking of gelatin using a simple plant-derived phenolic compound, caffeic acid has been studied. For the first time, we are reporting a thermo-irreversible gelatin gel formation at 60 °C. Controlling the crosslinking reaction has resulted in obtaining gelatin with modified material properties. Reaction parameters such as reaction pH, reaction time and concentration of caffeic acid have been optimised to obtain different degrees of crosslinking. The modified material properties were studied using small and large deformation rheology. Gelatin crosslinked at 60 °C and pH 9 for 20 min using 1.5% concentration of caffeic acid showed higher melting and setting temperatures. The storage modulus and gel strength were also found to be higher for crosslinked gelatin at higher temperatures.     

玉米麸皮不同处理及其成分分析

为探讨玉米麸皮的生理功能,需对玉米麸皮进行处理。通过酶处理除去玉米麸皮中含量较多的蛋白质和淀粉,得到精制玉米麸皮并确定最佳酶解工艺。再分别对精制玉米麸皮进行酸碱处理,得到相应的酸碱解产物。对玉米麸皮、精制玉米麸皮、酸解产物和碱解产物基本成分组成及膳食纤维组成进行分析。结果显示碱性蛋白酶去除玉米麸皮蛋白质的作用要好于酸性蛋白酶和中性蛋白酶。蛋白酶和淀粉酶能使玉米麸皮中的蛋白质和淀粉由10.32%和17.5%分别减少到1.65%和1.23%。精制玉米麸皮总膳食纤维比玉米麸皮增加26%。酸解产物和碱解产物基本成分是可溶性膳食纤维,其中可溶性半纤维素分别为83.52%和86.82%,不含纤维素和木质素。     

Chemical and physical modification of proteins by the hydroxide ion

Proteins are exposed to alkaline conditions during solubilization and/or purification, during food storage and processing, in removal of toxic constituents, and for characterization. During alkali treatment, there are changes in solubility and aggregation, hydrolysis, elimination reactions involving the side chains of certain amino acids, racemization of amino acid residues, addition of compounds to proteins, fragmentation of the peptide chain, as well as modification or elimination of nonprotein constituents. The rates of these reactions are affected by pH, temperature, cations (in some cases), ionic strength (in some cases), protein concentration, and to some extent by the specific nature of the protein. The general mechanisms and stoichiometry of these reactions are described. Other constituents of high protein foods also undergo reactions in alkaline solutions and the products of these reactions may in turn react with proteins. We have described the effect of alkali on enediol formation and fragmentation of carbohydrates, the hydrolysis of lipids in alkaline solution and effect on rate of peroxidation of the polyunsaturated fatty acids, the oxidation of amino acid residues, especially methionine, the oxidation of phenols to benzoquinones, and the catalytic effect of metal ions in alkaline solutions. Alkali treatment is also used in the specific modification of proteins to distinguish between O-glycosyl and amide-linked glycosyl groups, to effect specific cleavage of peptide bonds via beta elimination, in the formation of anhydrotrypsin, anhydrochymotrypsin, anhydrosubtilisin and thiol-subtilisin, and in formation of intrachain crosslinking in proteins.     

Characteristics of Gelatin from Giant Grouper (Epinephelus Lanceolatus) Skin

Gelatin extraction from the skin of giant grouper (Epinephelus lanceolatus) was conducted by acid process with a yield of 20.27 g/100 g wet skin sample. The characteristics of extracted gelatin from giant grouper was investigated in this study, and further compared to that from commercial tilapia. Results showed that when compared to commercial tilapia, giant grouper had lower levels of bloom strength and foam formation ability, but greater values of viscosity, foam stability, and lightness (L*) on gelatin skin. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis analysis revealed three high-bands intensities of major protein components of giant grouper skin gelatin, representing α1-chain, α2-chain, and β-components, and was similar to that of standard calf skin collagen type I. Compared to giant grouper, commercial tilapia contained extra proteins with molecular weight less than 70 kDa on the sodium dodecyl sulphate-polyacrylamide gel electrophoresis of both skin gelatins.