CN111621032A - Octenylsuccinic anhydride modified gelatin and preparation method and application thereof - Google Patents
Octenylsuccinic anhydride modified gelatin and preparation method and application thereof Download PDFInfo
- Publication number
- CN111621032A CN111621032A CN202010345460.3A CN202010345460A CN111621032A CN 111621032 A CN111621032 A CN 111621032A CN 202010345460 A CN202010345460 A CN 202010345460A CN 111621032 A CN111621032 A CN 111621032A
- Authority
- CN
- China
- Prior art keywords
- gelatin
- osa
- succinic anhydride
- octenyl succinic
- emulsion
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
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Links
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- Medicinal Preparation (AREA)
Abstract
The invention relates to the field of medical food additives, and discloses octenyl succinic anhydride modified gelatin. The preparation method comprises the following steps: (1) adjusting the pH value of the gelatin solution to 8-9, adding octenyl succinic anhydride under the stirring condition, and reacting for 2-6 h; the mass ratio of the octenyl succinic anhydride to the gelatin is 0.02-0.25: 1; (2) adjusting the pH value of the solution to 6-7; fractions of MW8000-14000Da were removed by dialysis. Octenyl succinic anhydride is mixed with a gelatin solution. The modified gelatin can be applied to the preparation of an emulsifier, and the emulsifier is applied to the preparation of emulsion, can obviously reduce the elutriation index and improve the stability of liquid drops, and has wide application prospect in the fields of food, medicine and the like.
Description
Technical Field
The invention relates to the field of medical food additives, in particular to an emulsifier, and particularly relates to an octenyl succinic anhydride modified gelatin used as an emulsifier.
Background
Fish oil has many important physiological and health functions for the human body, and is a good carrier for fat-soluble substances. However, fish oils have a fishy taste, are poorly water soluble and are susceptible to oxidation by environmental factors (pH, light, heat, etc.). Fish oil-loaded emulsions have great potential for reducing the application limitations of fish oils, and have attracted great attention over the last 20 years.
Mammalian and aquatic gelatins have been used as emulsifiers for o/w emulsions due to their excellent edibility, biocompatibility and degradability. Kraft gelatin and fish gelatin have been used to stabilize sunflower and corn oil as emulsifiers. The widespread use of mammalian gelatin has been limited due to mammalian disease and religious factors. Fish gelatin is considered as an alternative to mammalian gelatin. However, fish gelatin has lower gelling and rheological properties compared to mammalian gelatin, limiting its widespread use. Therefore, there is a need to find a method for modifying fish gelatin that is suitable for the development needs of the food industry.
Physical blending and chemical modification are two major modification methods to improve the properties of gelatin. Blending bovine bone gelatin with surfactants as emulsifiers has been studied for stabilizing fish oils. Furthermore, in the preparation of Pickering emulsions, gelatin is also prepared as crosslinked gelatin particles, gelatin/chitosan complexes or gelatin/glucomannan/tannic acid nanocomposites for encapsulating sunflower oil, fish oil, corn oil or medium chain triacylglycerol oil. Laccase is used for cross-linking pectin molecules when preparing fish skin gelatin-pectin multilayer emulsion, and the pH stability of the emulsion is improved. Various chemical modification methods have been used to modify fish skin gelatin, such as enzymatic, phosphorylation, aldehyde, and phenolic modifications. Wherein, phosphorylation modification can improve the stability of fish skin gelatin emulsion. Therefore, it is necessary to explore the application of other chemical modification methods in the field of emulsion.
Succinic anhydride modification has been applied to modify proteins such as soy protein isolate, infant protein concentrate, lentil protein concentrate and brazil nut lactoglobulin. These results indicate that the emulsification properties of succinylated proteins depend on protein concentration, pH and the degree of succinylation. However, succinic anhydride is classified as a 3-class carcinogen by the international cancer research institute of the world health organization in 2017, and the application of succinic anhydride in food is limited. Octenyl Succinic Anhydride (OSA) modification is used to modify starch, the carboxyl groups on OSA being esterified with the hydroxyl groups on the starch, the starch being in the form of polymorphous granules, and OSA-starch also being in the form of granules. Compared with succinic anhydride, OSA has different structural effects on modified protein due to acylation reaction between carboxyl and amino on amino acid with stronger reactivity on gelatin due to the existence of octenyl. Therefore, no protein has been modified by OSA as an emulsifier to stabilize emulsions.
Disclosure of Invention
The invention aims to provide an octenyl succinic anhydride modified gelatin.
The invention also provides a preparation method and application of the octenyl succinic anhydride modified gelatin.
The invention provides an emulsion containing the octenyl succinic anhydride modified gelatin.
The technical scheme is as follows: an octenyl succinic anhydride modified gelatin is characterized in that the succinylation degree is 29 to 100 percent. Preferably, the succinylation degree is 65% to 99%.
The gelatin is mammalian gelatin or aquatic gelatin.
Preferably, the mammalian gelatin is mainly derived from pig, cattle, chicken, rabbit, etc., and the extraction site is connective tissue such as bone, cartilage, skin, tendon, ligament, etc.; the aquatic gelatin is mainly derived from fish, sea cucumber, Stichopus japonicus, starfish, jellyfish, etc., the fish gelatin can be divided into warm water fish gelatin (such as tilapia, grass carp, longsnout catfish, silver carp, catfish, tuna, squid, etc.) and cold water fish gelatin (such as haddock, pollock, alaska cod, sturgeon, salmon, etc.), the extraction parts are fish skin, fish scale, fish bone, fish fin, swim bladder, fish head, etc., and the extraction parts of sea cucumber, Stichopus japonicus, jellyfish, starfish, etc. are mainly body wall.
Preferably, the mammalian gelatin is Bovine Bone Gelatin (BBG) and the marine gelatin is cold water fish skin gelatin (CFG) extracted from haddock, pollock, alaska cod, sturgeon or salmon.
The preparation method of the Octenyl Succinyl (OSA) modified gelatin comprises the following steps:
(1) adjusting the pH value of the gelatin solution to 8-9, adding octenyl succinic anhydride under the stirring condition, and reacting for 2-6 h;
the mass ratio of the octenyl succinic anhydride to the gelatin is 0.02-0.25: 1;
(2) adjusting the pH value of the solution to 6-7; fractions of MW8000-14000Da were removed by dialysis.
Preferably, the product of step (2) is freeze-dried.
Preferably, in step (1), the pH of the gelatin solution is 8.5.
Preferably, in step (2), the solution is adjusted to a pH of 6.5.
The concentration of the gelatin solution in the step (1) is 10-30 g/L, preferably 15-25 g/L, and more preferably 15-20 g/L.
The reaction in the step (1) is carried out at 0-40 ℃, preferably 20-35 ℃.
In a preferred embodiment of the present invention, the concentration of the gelatin solution of step (1) is 18 g/L.
The octenyl succinic anhydride modified gelatin is applied to the preparation of an emulsifier and the preparation of an emulsion, in particular a Pickering emulsion.
When the octenyl succinic anhydride modified bovine bone gelatin (OSA-BBG) is used as an emulsifier for reducing the creaming index, the succinylation degree of the octenyl succinic anhydride modified bovine bone gelatin (OSA-BBG) is 29-76%; when the method is used for improving the stability of liquid drops, the succinylation degree of the octenyl succinic anhydride modified bovine bone gelatin is 90-99%. For improving the droplet stability, it is preferable that the octenyl succinic anhydride-modified cold water fish skin gelatin (OSA-CFG) has a succinylation degree of 70% to 99%, more preferably 88% to 95%.
When the OSA-BBG with the succinylation degree of 29-76% is prepared, the mass ratio of octenyl succinic anhydride to bovine bone gelatin is 0.02-0.1; when the OSA-BBG with the succinylation degree of 90-100% is prepared, the mass ratio of the octenyl succinic anhydride to the bovine bone gelatin is 0.16-0.25.
The succinylation degree of the cold water fish skin gelatin modified by octenyl succinic anhydride is 70-99%, and the mass ratio of the octenyl succinic anhydride to the cold water fish skin gelatin is 0.1-0.25 during preparation.
The oil-carrying emulsion is characterized in that the octenyl succinic anhydride modified gelatin is used as an emulsifier, and the content of the octenyl succinic anhydride modified gelatin is 3-9 g/L, preferably 6-8 g/L, and more preferably 6-7 g/L based on the total volume of a water phase and an oil phase.
The oil is animal oil or vegetable oil. The animal fat is fish oil.
The oil-carrying emulsion also contains fat-soluble medicines or fat-soluble nutrient substances.
According to the preparation method of the oil-carrying emulsion, the pH value of the octenyl succinic anhydride modified gelatin solution is adjusted to 8.5-10, and the ratio of the pH value to the pH value of the octenyl succinic anhydride modified gelatin solution is 1: mixing oil or oil containing fat-soluble medicine or nutrient substances with the octenyl succinic anhydride modified gelatin solution according to the volume ratio of 1.5-3, and homogenizing. The concentration of the octenyl succinic anhydride modified gelatin solution is 5-12 g/L.
Preferably, the concentration of octenyl succinic anhydride modified gelatin solution is 10 g/L.
Preferably, the octenyl succinic anhydride modified gelatin solution is adjusted to a pH of 9 according to a 1: 2 volume ratio of the oil or oil containing fat-soluble drugs or nutrients and octenyl succinic anhydride modified gelatin solution are mixed and homogenized.
The homogenization conditions are 8000 to 15000rpm, preferably 10000 to 12000 rpm.
The OSA modified BBGs (OSA-BBGs) and OSA modified CFGs (OSA-CFGs) are prepared and characterized and used for the stable oil-carrying emulsion, and the result shows that the OSA modified gelatin can influence the stability of the oil-carrying emulsion.
OSA can be successfully used to modify gelatin and alter the isoelectric point of gelatin. Meanwhile, the succinylation degree and the mass ratio of OSA to gelatin increase logarithmically during the chemical modification. Furthermore, the OSA modification had no significant effect on the initial droplet size of the loaded fish oil emulsion, suggesting that the OSA modification did not alter the properties of the gelatin.
Emulsion storage experiments show that the emulsion prepared from the OSA-modified bovine bone gelatin has increased droplet stability, increased phase transition time and decreased creaming index with the increase of the succinylation degree, but the emulsion prepared from the OSA-modified fish skin gelatin only has increased droplet stability with the increase of the succinylation degree, and the phase transition time and the creaming index have no obvious change. The increased degree of succinylation may improve the droplet stability of the emulsion. Further, the phase transition time and creaming index of OSA-BBGs stable emulsions increase with increasing succinylation degree, but these two properties of OSA-CFGs stable emulsions are not significantly affected.
Thus, gelatin modified with octenyl succinic anhydride can significantly improve the stability of the emulsion. The octenyl succinic anhydride modified bovine bone gelatin OSA-BBG has better emulsion stability and can be used as a food emulsifier for beverages, dairy products and the like, and the octenyl succinic anhydride modified cold water fish skin gelatin OSA-CFG has better droplet stability and can be used as an emulsifier for encapsulating functional component emulsion.
The invention provides a molecular modification method of effective protein, the obtained modified gelatin emulsifier can effectively improve the emulsion stability, can optimize oil-carrying emulsion, especially fish oil-carrying emulsion, and has wide application prospect in the fields of food, medicine and the like; at the same time, it provides useful information for understanding the relationship between protein molecule modification, protein molecule structure and protein function. The method also provides a potential way for optimizing the preparation of the fish oil-carrying emulsion and the application of the fish oil-carrying emulsion in the fields of food and medicine.
Drawings
Fig. 1 shows a different OSA of example 1: characterization of the OSA modified gelatin prepared under the gelatin mass ratio; A-F are newly prepared OSA-BBGs solution, freeze-dried OSA-BBGs redissolution, newly prepared OSA-CFGs solution, freeze-dried OSA-CFGs redissolution solution, respectively, and glass bottles are arranged from left to right: 0.02, 0.05, 0.10, 016 and 0.21; g is different OSAs: the succinylation degree of the OSA modified gelatin prepared under the mass ratio of the gelatin; H-K is a graph of turbidity measurements for OSA-modified gelatin with a digital camera at different pH conditions (pH from left to right for vials in each graph: 3.0, 3.5, 4.0, 4.5, 5.0, and 5.5), H-I is OSA: OSA-BBGs with gelatin mass ratio of 0.05 and 0.16; J-K is OSA: OSA-CFG with gelatin mass ratio of 0.05 and 0.16.
Fig. 2 shows unmodified gelatin (i.e. 0.00) and different OSA: digital camera and optical microscopy images of OSA-modified gelatin-stabilized emulsions prepared at gelatin mass ratios (0.02, 0.05, 0.10, 016 and 0.21) at the initial stage of preparation; the scale bar is 50 μm.
Fig. 3 shows unmodified gelatin (i.e. 0.00) and different OSA: the CLSM pattern of stable OSA-modified gelatin emulsions prepared at gelatin mass ratios (0.02, 0.05, 0.10, 016 and 0.21) at the initial stage of preparation. Staining fish oil with nile red; the scale bar is 25 μm.
FIG. 4 is the most likely particle size distribution of OSA-BBGs stabilized emulsions (A) and OSA-CFGs stabilized emulsions (B), 0.00 indicating that the emulsions are stabilized by unmodified gelatin.
FIG. 5 shows a representative droplet size distribution of OSA-BBGs stabilized fish oil-loaded emulsions at the initial stage of production. A: unmodified BBG stable emulsions. B-F: different OSAs: OSA modified BBGs stable fish oil-carrying emulsions prepared at gelatin mass ratios (0.02, 0.05, 0.10, 016 and 0.21); peak 1, peak 2, and peak 3 are gaussian fit lines.
FIG. 6 shows a representative droplet size distribution of OSA-CFGs stabilized fish oil-loaded emulsions at the initial stage of production. A: unmodified BBG stable emulsions. B-F: different OSAs: OSA modified BBGs stable fish oil-carrying emulsions prepared at gelatin mass ratios (0.02, 0.05, 0.10, 016 and 0.21); peak 1, peak 2, and peak 3 are gaussian fit lines.
Fig. 7 shows unmodified gelatin (i.e. 0.00) and different OSA: digital camera and optical microscopy images of OSA-modified BBG-stabilized emulsions prepared at gelatin mass ratios (0.02, 0.05, 0.10, 016 and 0.21) during storage at 4 ℃. Black arrows indicate creaming layers at creaming values > 7.0%, black stars indicate the creaming gel; the scale bar is 50 μm.
Fig. 8 shows unmodified gelatin (i.e. 0.00) and different OSA: digital camera and optical microscopy images of OSA modified CFG stable emulsions prepared at gelatin mass ratios (0.02, 0.05, 0.10, 016 and 0.21) during storage at 4 ℃. Black arrows indicate creaming layer at emulsion creaming value > 7.0%, white stars indicate syrupy emulsion; the scale bar is 50 μm.
Fig. 9 shows unmodified gelatin (i.e. 0.00) and different OSA: digital camera and optical microscopy images of OSA-modified BBG-stabilized emulsions prepared at gelatin mass ratios (0.02, 0.05, 0.10, 016 and 0.21) stored at 4 ℃ for 3 days and 14 days. Black arrows indicate creaming layers at creaming values > 7.0%, black stars indicate the creaming gel; the scale bar is 50 μm.
Fig. 10 shows the unmodified gelatin (i.e. 0.00) and OSA as distinct OSA: digital camera and optical microscopy images of OSA modified CFG stable emulsions prepared at gelatin mass ratios (0.02, 0.05, 0.10, 016 and 0.21) stored at 4 ℃ for 3 days and 14 days. Black arrows indicate creaming layers at a creaming value > 7.0%; the scale bar is 50 μm.
Fig. 11 shows different OSAs: OSA-BBGs (A) and OSA-CFGs (B) prepared under the gelatin mass ratio (0.02, 0.05, 0.10, 016 and 0.21) stable fish oil-carrying emulsion has the milk precipitation index during storage at 4 ℃; 0.00 represents an emulsion stabilized by unmodified gelatin.
Fig. 12 is a schematic diagram of the mechanism of OSA-modified gelatin and its use in fish oil-loaded emulsions, (a): succinylation of OSA and gelatin; (B) the method comprises the following steps Unmodified and OSA modify the molecular structure of gelatin, showing a degree of succinylation that varies with OSA: the mass ratio of the gelatin is increased in a logarithmic scale, and the molecular volume of the gelatin is increased along with the increase of the succinylation degree, so that the OSA-CFGs has higher OSA group ratio on the surface-core of the molecule than the OSA-BBGs; (C) the method comprises the following steps Unmodified and OSA-modified gelatin-stabilized emulsion droplets, OSA-CFGs-stabilized emulsion droplets having a higher negative charge and greater resistance to droplet coalescence than OSA-BBGs-stabilized emulsion droplets, the degree of succinylation having no significant effect on the initial emulsion droplet size.
Detailed Description
Materials: BBG (type B, 240g bloom) and CFG are purchased from Alantin Biotechnology, Inc. (Shanghai, China), Sigma-Aldrich (Shanghai, China), respectively; deep sea fish oil (food grade, DHA + EPA > 70%) is purchased from Qianye grass Biotechnology GmbH of Xian (Shaanxi, China) and stored at-18 deg.C; OSA is purchased from shanghai-sourced leaf biotechnology limited (shanghai, china); all chemicals were purchased from the national pharmaceutical group chemical agents limited (shanghai, china).
Example 1 preparation of OSA-BBG and OSA-CFG
Determination of amino acid content
Amino acid content of Bovine Bone Gelatin (BBG) and cold water fish skin gelatin (CFG) was determined by weighing 1.0g of gelatin powder (BBG and CFG) into a 30mL hydrolysis tube and immediately adding 10mL of HCl (6mol/L) and 0.15mL of phenol. The sample was refrigerated at 4 ℃ for 5 min. The sample was then evacuated for 10min and hydrolyzed at a temperature of 110 ℃ for 22 h. The hydrolysate was filtered through filter paper, collected in a 50mL volumetric flask and made up to 50mL with ultra pure water. The sample after vacuum drying was dissolved in a mixture of 20mL of sodium citrate buffer (66.6mM, pH 2.2) and ultrapure water at a volume ratio of 1: 19. Samples and commercial mixed amino acid standards (sigma-Aldrich, USA) were analyzed using a fully automated amino acid analyzer model L-8800. Each set of samples was measured 3 times in parallel and the results are shown in table 1.
TABLE 1 amino acid mass percent of gelatin
The results show that BBG and CFG have different contents of methionine, serine, histidine, threonine and proline.
(Di) octenyl succinic anhydride modification
Bovine Bone Gelatin (BBG) and cold water fish skin gelatin (CFG) were dissolved in a water bath at 45 ℃ and 180rpm for 60min to obtain BBG and CFG solutions (1.8%, w/v). The gelatin solution was adjusted to pH 8.50 with 1M HCl and 1M NaOH using a pH meter. The gelatin solution was magnetically stirred at 35 ℃ and 300 rpm. OSA was slowly added to the gelatin solution such that the mass ratio of OSA to gelatin was 0.02, 0.05, 0.10, 0.16, and 0.21. Then, the solution pH was maintained in the range of 8.50-9.00. After 3 hours of reaction, the solution was adjusted to pH 6.50 to terminate the reaction. The resulting solution of the reaction was dialyzed with ultrapure water for 24 hours (MW: 8000-. Finally, the solution was vacuum freeze-dried to obtain purified OSA-BBGs and OSA-CFGs, and the results of the freeze-dried OSA-BBGs and the freeze-dried OSA-CFGs are shown in fig. 1B and fig. 1E, respectively. The lyophilized powder was reconstituted with ultrapure water to give a 1.0% (w/v) solution (1g/100mL), and the results are shown in FIG. 1D and FIG. 1F, respectively, which illustrate that the lyophilized powder has good solubility in pure water.
OSA-modified gelatin solutions and solid samples were tested in high OSA: gelatin mass ratio is pink, while at low OSA: the solution prepared under the gelatin mass ratio condition is transparent, and the solid is white. Ninhydrin colorimetric assay of succinylation results showed that the succinylation degree of OSA-modified gelatin varies with OSA: the increase in the gelatin mass ratio tended to increase logarithmically (fig. 1G). The UV absorbance of the unmodified BBG (1.21. + -. 0.01) was higher than that of the unmodified CFG (1.08. + -. 0.01) as measured by ninhydrin colorimetry, due to the higher lysine mass fraction of BBG than CFG (Table 1).
OSA-modified gelatin in OSA: gelatin mass ratios of 0.02, 0.05, 0.10, 0.16 and 0.21 (fig. 1). The solutions obtained by modifying OSA with gelatin (FIGS. 1A and 1D) were freeze-dried to obtain solid samples (FIGS. 1B and 1E), and these solid samples were reconstituted with ultrapure water to obtain 1.0% (w/v) solutions (FIGS. 1C and 1F). The succinylation reaction of gelatin and OSA is shown in fig. 12A.
(III) determination of the degree of succinylation
The method for measuring the succinylation degree refers to the existing method and is slightly modified. Briefly, the ninhydrin solution was prepared by dissolving 0.5g of ninhydrin hydrate, 10.0g of disodium hydrogen phosphate dodecahydrate, 6.0g of potassium dihydrogen phosphate and 0.3g D-fructose (Shanghai Michelin Biochemical technology Co., Ltd.) in 50mL of ultrapure water and making a volume of 100mL with ultrapure water. 2mL of the ninhydrin solution was added to 2mL of a 1mg/mL OSA-modified gelatin solution. The mixed solution was boiled for 15min and then immediately cooled in water at 4 ℃. After cooling, 6mL of ethanol solution (50%, v/v) was added. The absorbance of the solution was measured at 570nm with an ultraviolet spectrophotometer (New century T6, Beijing Punja instruments Ltd., China) and unmodified gelatin was used as a control. Each set of samples was measured 3 times in parallel. And the succinylation Degree (DS) was calculated as follows:
wherein A is0And A1Absorbance values for unmodified gelatin and OSA modified gelatin were determined, respectively.
Different OSAs: the succinylation degree results of OSA-modified gelatin prepared by mass ratio of gelatin are shown in fig. 1G and table 2. The data were fitted using a logarithmic equation, the fitting equation for OAS-BBG: y 143.79+30.73 ln (x + 0.01); fitting equation for OAS-CFG: y 143.29+32.01 × ln (x + 0.01).
TABLE 2
The OSA-CFG succinylation degree is slightly lower than that of OSA-BBG at the same OSA-gelatin mass ratio.
(IV) turbidity assay of OSA-modified gelatin
Turbidity analysis of OSA-modified gelatin was performed by reference to existing methods. Briefly, the pH of a 5% (w/v) gelatin solution was adjusted to different pH (3.0, 3.5, 4.0, 4.5, 5.0, 5.5) and the solution was immediately observed and captured with a digital camera. The results are shown in FIGS. 1H-K, with the pH from left to right for the vials in each figure: 3.0, 3.5, 4.0, 4.5, 5.0 and 5.5. H and I are OSA: turbidity measurements of OSA-BBGs with gelatin mass ratio 0.05 and 0.16, J and K are OSA: OSA-CFGs turbidity measurements of gelatin mass ratios 0.05 and 0.16.
Turbidity was measured for both OSA-modified gelatins in order to analyze the effect of succinylation degree on isoelectric point of OSA-modified gelatins. The results show that when OSA: at a gelatin mass ratio of 0.05, OSA-BBG became cloudy at pH 3.5-4.5 (FIG. 1H), and OSA-CFG became cloudy at pH 4.0-4.5 (FIG. 1J). When the OSA: at a gelatin mass ratio of 0.16, turbidity became cloudy at pH 3.0-5.0 and was significantly higher at pH3.0-4.5 than at pH 5.0 (fig. 1I, 1K). Meanwhile, OSA-BBGs are more turbid than OSA-CFGs.
And (4) conclusion: effect of OSA modification on gelatin Structure
Succinylation is a molecular modification method. OSA reacts primarily with the-amino group of lysine and secondarily with the N-terminal amino acid in the protein, converting it from a positively charged residue to a negatively charged residue by N-acylation. In this experiment, both BBG and CFG are subject to different OSA: the gelatin mass ratios (0.02, 0.05, 0.10, 0.16 and 0.21) and OSA were succinylated (fig. 1A-1F). The succinylation reaction of gelatin and OSA is shown in fig. 12A.
The results show that the degree of succinylation of gelatin varies with OSA: the increase in the gelatin mass ratio increased logarithmically (fig. 1G). BBG is higher in lysine mass percentage than CFG (table 1), and succinylation significantly enhances the electrostatic repulsion within the molecule, possibly causing conformational changes and decomposition such as molecular volume increase. With OSA: the gelatin mass ratio increases and the degree of succinylation increases (fig. 1G), and thus, the gelatin molecular volume may increase. Considering that BBG becomes cloudy at pH 5.0 and CFG is visibly cloudy at any pH range, OSA modification dramatically changed the isoelectric point of BBG and CFG (fig. 1H-1K), probably because the positive charge of lysine was converted to the negative charge of OSA. Finally, considering that the molecular weight of BBG is significantly higher than that of CFG, the molecular structure of OSA-modified gelatin is shown in fig. 12B.
Example 2 preparation of OSA-modified gelatin-stabilized Fish oil-loaded emulsion
The unmodified and OSA-modified gelatin solutions of different succinylation degrees prepared in example 1 (1.0%, w/v) were dissolved and the pH of the solution was adjusted to 9.0. According to the following steps of 1: 2 to the gelatin solution. Then use
Homogenizing with a homogenizer at 11500rpm for 1 min. The resulting emulsion was stored at 4 ℃. The emulsion was observed with a digital camera, optical microscope and scanning laser confocal optical microscope (CLSM).
(I) detection method
1. Observation with an optical microscope
A3. mu.L sample of the liquid emulsion was dropped onto a glass slide, covered with a cover slip, and observed with an inverted optical microscope (MS600F, Shangham Minitz precision instruments Co., Ltd., China). Approximately 3mg of the latex gel sample was cut and placed on a glass slide, covered with a cover slip, and observed with a vertical optical microscope (ML8000, Shangham Mingzi precision instruments Co., Ltd., China). The objective lenses of the inverted optical microscope and the upright optical microscope were 50 × and 60 ×, respectively. The droplet size was statistically analyzed using gaussian fitting.
2. Milk analysis index determination
The height of the creaming layer (H) of the emulsion stored at 4 ℃ was measured at the indicated time points (0H,3H,3d,7d,14d,21d, and 28d)s) And the total height of the emulsion (H)t). Milk analysis index was calculated as follows:
CLSM Observation
Liquid samples at the initial stage of preparation were observed by laser confocal scanning microscopy (CLSM) with reference to the previous work in the laboratory. Briefly, 40. mu.L of Nile Red in 1, 2-propanediol (0.1%, Biotechnology engineering (Shanghai) Co., Ltd., China) was added to 1mL of the liquid emulsion. After 5min, 3. mu.L of the mixed sample was dropped onto a glass slide, covered with a cover glass, and observed with a confocal laser scanning microscope (model TCS SP 8; Leica, Wetsland, Germany). Nile red (fish oil) was excited at a wavelength of 552nm and observed using a 63 x oil mirror. The scanning frequency was 100Hz and the scanning density was 1024X 1024.
4. Gaussian fitting of droplets
Gaussian fitting of droplet size was performed with reference to previous work in this laboratory, and MeizsMcs 6.0 software (Shangham Mintiz precision instruments, Inc., China) was used to measure the size of approximately 400-. The droplet size was statistically analyzed by frequency distribution. The number of the columns is 25-30. Finally, the possible multimodal distribution of droplet sizes was analyzed using multimodal gaussian fit. The results are shown in the figure.
And (3) data analysis: the data above are presented as mean ± standard deviation of three replicates. Statistical comparisons were performed using one-way anova. A p value <0.05 was considered a significant difference.
(II) results
Characterization of OSA-modified gelatin-stabilized Fish oil-loaded emulsions at the initial stage of preparation
Gelatin tends to agglomerate when the emulsion pH approaches the isoelectric point of the gelatin. In general, strongly alkaline foods are not common and only a few weakly alkaline foods, such as water at pH 9.5, are present in the world. Based on the isoelectric point of OSA-modified gelatin (FIGS. 1H-1K) and previous work in this laboratory, a fish oil-loaded emulsion stabilized by OSA-modified gelatin was prepared by homogenization at pH 9.0. The emulsion at the beginning of the preparation appeared milky white and consisted mainly of micron-sized droplets (fig. 2). The CLSM experimental results showed that fish oil was present in the droplets (fig. 3). The representative droplet size distribution showed a trimodal droplet size distribution with no significant difference in the frequency of the three peaks (fig. 4-6), indicating OSA: the gelatin mass ratio and the degree of succinylation had no significant effect on the initial droplet size. Peak 3 (Peak maximum) of the OSA-BBGs stable emulsion was lower than peak 3 (Peak maximum) of the OSA-CFGs stable emulsion, while Peak 1 and Peak 2 values were similar (FIG. 4).
Storage stability of OSA-modified gelatin-stabilized fish oil-loaded emulsions
The creaming stability and droplet stability of OSA-modified gelatin stabilized fish oil-loaded emulsions stored at 4 ℃ were observed to analyze the liquid-gel phase transition behavior, droplet coalescence behavior and the change in creaming index values (fig. 7-11). For OSA-BBGs stable emulsions, with OSA: increasing the gelatin mass ratio and the degree of succinylation increases the liquid-gel phase transfer time (FIG. 7: digital camera image; 3 days at mass ratio 0.00-0.05; 7 days at mass ratio 0.10; 21 days at mass ratio 0.16 and 0.21), the droplet coalescence is slowed down (FIG. 7: optical microscope image), and the value of the milk index increases (FIG. 11A). All OSA-CFG stable emulsions became syrupy by 28 days of storage (FIG. 8: digital camera images) and had similar changes in the creaming index values (FIG. 11B). Thus, with OSA: the increased gelatin mass ratio and succinylation degree had no significant effect on these properties of the OSA-CFG stable emulsion. However, with OSA: the gelatin mass ratio and the degree of succinylation increased the droplet coalescence of the OSA-CFG stable emulsion was slower (FIG. 8: light microscopy).
(III) analysis and discussion
Effect of OSA modification on Primary droplet size
All emulsion droplets made with unmodified and OSA-modified gelatin exhibited a trimodal particle size distribution (similar frequency) and OSA: the gelatin mass ratio had no significant effect on the primary droplet size (fig. 2, 4, 5, 6). The primary particle size of the emulsion prepared by the homogenization process depends on the nature of the emulsifier, the energy input, the dispersed phase concentration, the temperature and the viscosity of the emulsion. The fish oil-loaded emulsions at the beginning of these preparations differed only by the emulsifier (gelatin and OSA-modified gelatin). Therefore, OSA modification did not alter the properties of gelatin for emulsion droplet formation, which is probably due to the low lysine mass percentage of gelatin (4.36% ± 0.02% BBG, 4.02% ± 0.01% CFG), as shown in table 1.
Effect of OSA modification on droplet coalescence
Coalescence of droplets occurs when the attractive force between the droplets is greater than the repulsive force. In a typical droplet coalescence process, two or more droplets come into close proximity and the interfacial layer around the droplets breaks up and the droplets merge together to form one larger droplet. In this experiment, with OSA: the increase in the gelatin mass ratio, the degree of succinylation increased (FIG. 1G), and the amount of negative charge of the gelatin shell layer increased. Therefore, the repulsive force between the droplets increases. In so doing, droplet coalescence is reduced (FIGS. 7-10). This means that, with OSA: the gelatin mass ratio increases the droplet stability. CFG has a lower molecular weight, so OSA-CFGs have a higher surface area to volume ratio than OSA-BBGs. Therefore, although OSA-CFGs have a lower succinylation degree than OSA-BBGs, OSA-CFGs have a higher OSA group ratio on the surface-core of the molecule than OSA-BBGs. As such, OSA-CFGs exhibited higher resistance to droplet coalescence than OSA-BBGs (fig. 7-10), which is consistent with the comparison of unmodified BBG-stabilized emulsions and unmodified CFG-stabilized emulsions in this experiment (fig. 7-8) and the work prior to this laboratory. According to the above analysis, OSA-CFGs have better droplet stability than OSA-BBGs and droplet stability increases with increasing succinylation degree of gelatin.
Effect of OSA modification on emulsion liquid-gel transition
Emulsions can be classified into liquid and gel forms according to the state of the emulsion. Emulsion gel both emulsion and gel are present. Emulsion gels can be divided into emulsion filled but comparable gels (the continuous phase is coagulated) and protein stabilized emulsion gels (the emulsion droplets are aggregated). The pre-lab CLSM results show that BBG and CFG are mainly present in the shell of the droplets and that almost no free gelatin is present in the continuous aqueous phase. Thus, the emulsion gel stabilized by gelatin and OSA modified gelatin in this experiment was likely a protein stabilized emulsion gel, which was likely produced by emulsion droplet aggregation.
For OSA-BBG stable emulsions prepared at pH 9.0, the ratio of emulsion with OSA: the gelatin mass ratio increased, the succinylation degree increased (fig. 1G), the amount of negative charge of the shell layer increased and the repulsion between droplets increased. Thus, with OSA: the increased mass ratio of gelatin, decreased the OSA-BBG stable emulsion droplet aggregation behavior and increased the liquid-gel transition time (fig. 7, 10). For the OSA-BBG stable emulsion prepared at pH 9.0, the liquid-gel transition hardly occurred and only converted to a syrupy emulsion (FIG. 8), which further confirms that OSA-CFGs have a higher ratio of negatively charged OSA groups on the molecular surface-core than OSA-BBGs. Based on these projections, the molecular structure of OSA-modified gelatin is shown in fig. 12B.
Effect of OSA-modified gelatin on creaming stability
The speed of movement of individual droplets in an emulsion can be expressed in Stokes' equations:
where the minus sign indicates the direction of movement of the droplet, g is the acceleration of gravity, r is the radius of the droplet, ρ is the density, η is the shear viscosity, and subscripts 1 and 2 refer to the continuous and dispersed phases (droplets), respectively.
Density of dispersed phase (p)2) Can be expressed by the following equation:
where r is the initial drop radius, ρcoreIs nuclear layer oil density, ρshellIs the interface shell density and is the interface shell thickness.
For micro-scale droplets, the interfacial shell thickness (in the nanometer scale) is significantly lower than the initial droplet radius (r, in the micrometer scale). Equation (5) can be expressed approximately as the following equation:
in the present invention, the creaming index value of OSA-modified gelatin-stabilized emulsions increased with increasing storage time at 4 ℃ (fig. 11). In addition, the OSA-BBG stabilized emulsion had a lower creaming index value than the OSA-CFG stabilized emulsion (fig. 11), which is consistent with the results of comparing unmodified BBG stabilized emulsions and unmodified CFG stabilized emulsions in previous work in this laboratory.
BBG and OSA-BBGs stabilized emulsions have similar initial droplet radii (r, FIGS. 2, 4, 5), shell fish oil densities (p;)core,901kg/m3) Shear viscosity of continuous phase (η)1) And continuous aqueous phase density (p)1). BBG interface layer density is usually 1350kg/m3. OSA-BBGs stable emulsions with increasing interfacial shell density (ρ) with conformational changes and dissociation of the moleculeshell) Decrease and increase of interfacial shell thickness () (fig. 12B). According to equation (5), with OSA: increased mass ratio of gelatin and succinylation degree, OSA-BBG stable emulsion dispersionDensity (p)2) And decreases. Furthermore, the dispersed phase density (ρ) is compared to the BBG interface layer density2) In the low OSA: there was a slight increase in gelatin mass ratio (0.02, 0.05, 0.10) and, at high OSA: the mass ratio of gelatin (0.16, 0.21) was reduced. According to equation (3), with OSA: the gelatin mass ratio and the succinylation degree increased, the final creaming speed value increased, and BBG-stabilized emulsions had improved stability at low OSA: gelatin mass ratio (0.02, 0.05, 0.10) and high OSA: there are medium-rate creaming values between the gelatin mass ratios (0.16, 0.21). Thus, with OSA: the gelatin mass ratio increased, the final creaming index of the BBG stable emulsion increased, and the BBG stable emulsion had a low OSA: gelatin mass ratio (0.02, 0.05, 0.10) and high OSA: there was a moderate final milk out index between the gelatin mass ratios (0.16, 0.21) as shown in table 3 and fig. 11A.
Similar to OSA-BBGs, according to equation (3-5), as OSA: gelatin mass ratio and degree of succinylation increase the final milk out rate value of OSA-CFGs stable emulsions increases. Given the higher ratio of OS groups on the surface-core of the molecule for OSA-CFGs than for OSA-BBGs (fig. 12B), OSA-CFGs stable emulsions have higher negative charge and droplet anti-coalescence capabilities (fig. 12C), which may negate the effect of the creaming rate on the creaming of OSA-CFGs stable emulsions. Thus, all CFG and OSA-CFGs stabilized emulsions have similar creaming index changes, as shown in FIG. 11B.
TABLE 3 milk analysis index (%). of OSA-BBG and OSA-CFG on different days of storage at 4 ℃
5. Conclusion
Characterization of the OSA modification indicated the degree of succinylation of the gelatin during the chemical reaction and OSA: the gelatin mass ratio increases logarithmically. Characterization of fish oil-loaded emulsions stabilized for OSA-modified gelatin showed that the degree of succinylation had no significant effect on the initial emulsion droplets, suggesting that OSA modification did not alter the properties of the gelatin. The increased degree of succinylation may improve the droplet stability of the emulsion. Further, the phase transition time and creaming index of OSA-BBGs stable emulsions increase with increasing succinylation degree, but these two properties of OSA-CFGs stable emulsions are not significantly affected. The present study provides an efficient molecular modification method for modifying gelatin and provides useful information for understanding the effect of molecular modification on the functional properties of OSA-modifying proteins. The stable fish oil-carrying emulsion of the OSA modified gelatin has wide application prospect in the fields of food, medicine and the like.
Claims (10)
1. An octenyl succinic anhydride modified gelatin is characterized in that the succinylation degree is 29-99%.
2. The octenyl succinic anhydride modified gelatin of claim 1, wherein the gelatin is a mammalian gelatin or an aquatic gelatin.
3. The method of preparing octenyl succinic anhydride modified gelatin according to claim 1, comprising the steps of:
(1) adjusting the pH value of the gelatin solution to 8-9, adding octenyl succinic anhydride under the stirring condition, and reacting for 2-6 h; the concentration of the gelatin solution is 10-30 g/L;
(2) adjusting the pH value of the solution to 6-7; fractions of MW 8000-.
4. The process according to claim 3, wherein in the step (1), the gelatin solution has a pH of 8.5; in step (2), the pH of the solution was adjusted to 6.5.
5. The use of octenyl succinic anhydride modified gelatin of claim 1 for the preparation of an emulsifier or emulsion.
6. The use according to claim 5, wherein the gelatin is bovine bone gelatin or cold water fish skin gelatin, and the octenyl succinic anhydride modified bovine bone gelatin has a succinylation degree of 29 to 70% or 90 to 99%; the cold water fish skin gelatin succinylation degree modified by the octenyl succinic anhydride is 70 to 99 percent.
7. An oil-carrying emulsion, characterized in that the octenyl succinic anhydride modified gelatin of claim 1 or 2 is used as an emulsifier, the octenyl succinic anhydride modified gelatin content is 3-9 g/L based on the total volume of the water phase and the oil phase, and the oil is animal oil or vegetable oil.
8. The oil-in-water emulsion of claim 7, further comprising a fat-soluble drug or a fat-soluble nutrient.
9. The oil-loaded emulsion of claim 7 or wherein the animal fat is fish oil.
10. The method for producing an oil-loaded emulsion according to claim 7, wherein the pH of the octenyl succinic anhydride-modified gelatin solution is adjusted to 8.5 to 10 in a range of 1: mixing oil or oil containing fat-soluble medicine or nutrient substances with the octenyl succinic anhydride modified gelatin solution according to the volume ratio of 1.5-3, and homogenizing.
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