Abstract: Algae, as a kind of cultured objects with economic value, are widely cultivated in the world. Phycocyanin, a light-energy pigment in the gallbladder of algae, has received more and more attention for its natural blue color and wide range of physiological properties, and its physiological functions, such as anti-inflammatory, anti-tumor, antioxidant, and immunomodulatory, have been fully verified. However, purified phycocyanin is prone to precipitation or dissociation after water solubilization, and shows strong sensitivity to environmental factors such as temperature, pH value, light, and ions. In terms of its color stability, the stability of phycocyanin is improved by nanostructures such as particles and emulsions, so as to maintain its stability during food processing, production, storage and transportation.
.jpg)
In terms of maintaining its activity, the bioavailability of phycocyanin can be improved by physical and chemical modification of phycocyanin or delivery of phycocyanin through the construction of nanocarriers. In addition, phycocyanin has the characteristics of fluorescent macromolecule, which can be applied in the fields of nanowalls, metal nanoparticles, fluorescent probes, etc. This review summarizes the existing research results. This review summarizes the existing research results and provides a reference for the development and utilization of algal blue protein.
Spirulina platensis or Arthrospi- ra platensis is cultured on a large scale worldwide and has great economic and development potential as a source of functional factors, drugs and fluorescent substances [1]. In its dry matter, protein accounts for 55%~70%, and Phycobiliprotein accounts for 15%~20% of the total protein [2], mainly in the form of Phycocyanin (PC). Phycocyanin is a kind of chromoprotein that absorbs and transmits light energy in algal organisms. It absorbs orange-yellow light and shows a natural bright blue color, with the maximum absorption peak at a wavelength of about 620 nm. Using the water-soluble property of phycocyanin, microalgae cells were crushed and then industrially produced by salinization, extraction or chromatography to obtain purified phycocyanin, and the purity of the protein was classified into food grade (≥0.7), reaction grade (≥3.9), and analytical grade (≥4.0) according to the ratio of absorbance A620 nm/A280 nm [3].
1 Introduction to algal blue protein
Phycocyanin exists in microalgae cells in the form of assembled phycobilisome (PBS), and the light energy absorbed by the phycobilisome is transmitted through phycoerythrin (PE), phycocyanin, and allophycocyanin (APC) in order to reach the reaction center photosystems I and II[4] . The secondary structure of phycocyanin is dominated by the α-helix, which accounts for more than 60%[5] , and its high level structure is composed of (αβ) heterodimer units, the α-subunit has a molecular mass of 12~19 ku, containing two cysteine residues and two methionine residues; the β-subunit has a molecular mass of 14~21 ku, containing three cysteine and five methionine residues, and the β-subunit is composed of a (αβ) 3-cyclic trimer and (αβ) 3-cyclic trimer under physiological conditions. Under physiological conditions, (αβ) 3-cyclic trimer and (αβ) 6-cyclic hexamer are the main forms of phycocyanin [6]. The hexamer has a molecular mass of about 104 ku, and the αβ-subunits are bound by α-helix-mediated interactions. The chromophore in the molecular conformation of phycocyanin is called phycocyanin, which is a linear tetrapyrrole (porphyrin) compound connected to cysteine residues on the de-coordinated protein chain by thioether bonds, and the connection sites are generally at α-84, β-84, and β-155 [7], and the water molecules as a hydrophilic protein can further stabilize the phycocyanin coloration. As a hydrophilic protein, water molecules can further stabilize the chromophore conformation of phycocyanin and the interaction between the chromophore and cysteine residues.
Algae cyanine has various physiological functions such as anti-inflammatory, anti-tumor, antioxidant, immunomodulatory and so on [8-10], and a large number of researches have been reported on its anti-lung cancer, anti-melanoma, anti-colon cancer, and anti-hepatocellular carcinoma activities [11]. The industrial preparation of food-grade algal blue protein will gradually become a convenient and low-cost technology. The use of phycocyanin as a functional food or food ingredient is promising. However, the stability of phycocyanin is easily affected by factors such as temperature, pH, light, ions, etc. It is very sensitive to processing conditions, such as pasteurization, acidification and oxygenation, which may lead to degradation by precipitation or dissociation, and the blue color loses stability, which ultimately leads to the limitation of its application in the food industry.
Kupka et al [12] induced monomerization of alginate hexamers by increasing the concentration of urea in the system until the loss of its secondary structure .
This study analyzed the relationship between the molecular conformation of phycocyanin and the changes in the high-level structure of phycocyanin during this process, and explored the process in which the chromophore of phycocyanin trimer (αβ) 3 starts to lose its chromophore function after depolymerization and partial unfolding until the secondary structure of the protein is lost completely.Ma et al. [13] reported that the β-subunit of natural phycocyanin undergoes a three-step reversible conformational change during the folding and unfolding of β-subunits, and the refolding of the β-subunits is an example. Taking the refolding of β-subunit as an example, the tetrapyrrole chromophore first changes from a helical conformation to an extended conformation; through hydrogen bonding and hydrophobic interactions, the chromophore is fixed to the β-subunit with a more rigid structure, resulting in a linear increase in fluorescence; the relative motion between the subunits brings the two chromophores closer to each other or parallel to each other, and the fluorescence properties of the chromophore are enhanced.
Tong et al. [14] applied three kinds of proteases to enzymatically cleave phycocyanin to generate peptides with residues less than 63, and then analyzed the effects of the binding site and molecular configuration changes between tetrapyrrole chromophore and de-coordinating proteins on the color of phycocyanin. In addition, in the evaluation of the thermal stability of phycocyanin, the occurrence of the "hyperchromatic phenomenon", i.e., an increase in absorbance in the first few minutes of heat treatment followed by a decrease in absorbance, has been reported in many papers [5, 12]. This phenomenon reflects a change in protein structure, with conformational changes and denaturation of intermediate subunits leading to exposure of aromatic groups and shifting of chromophore sites before denaturation and aggregation of natural proteins begin.
For the use of alginate, Nourmohammadi et al. [15] attempted to encapsulate Arthrospira platensis with alginate and whey proteins as a functional ingredient and colorant in skimmed yogurt. Effective embedding of Arthrospira platensis was achieved by electrostatic interactions between the wall materials and full release in simulated gastrointestinal digestion, which increased bioavailability and facilitated the colonization of lactobacilli in the human gut.Dev et al.[16] combined carrageenan with alginate to prepare a hemostatic gel. The hydrogel showed a homogeneously distributed macroporous structure and was biocompatible, allowing nutrient transport and gas exchange at the wound healing site, thus promoting cell proliferation and wound healing.
In addition, as shown in Table 1, there are numerous reports on the incorporation of algal cyanobacteria or Spiroplasma obtusum as a raw material into food matrices, where the natural blue color of algal cyanobacteria imparts pure color and certain antioxidant properties to the product. Nevertheless, the development of the functional properties and coloring potential of algal cyanobacteria still needs to be continued, and there is still room for optimizing the pigment stability of algal cyanobacteria. In the face of the rapidly growing global market for natural colorants, alginate has been patented and its application in the medical field has been developing rapidly[17] . In this context, the development of blue pigments based on phycocyanin and their delivery systems as active ingredients has a broad application prospect.
2 Application of algal blue protein pigments
The color blue in food gives the impression of freshness and coolness, and the scarcity of blue substances in nature has made algal cyanoproteins one of the limited options for a natural source of blue color in the food industry [31]. Artificial cultivation of algae has made it economical and convenient to obtain algal cyanin extracts. On the basis of one-step and two-step culture methods, Chentir et al.[2] achieved a significant increase in algal cyanin production up to 230.1 mg/g dry matter by applying environmental stresses to change the accumulation of metabolites and reduce biological consumption. At present, the blue pigments allowed to be added to foodstuffs in China are synthetic indigo and brilliant blue (and their color precipitates), and gardenia blue and alginate blue (alginate protein) from natural sources [32]. In addition, some anthocyanins can also be used as blue coloring agents in food under certain conditions.
In water or phosphate buffer, it is difficult to maintain the stability of purified phycocyanin for a long time. With the continuous depolymerization of phycocyanin subunits, the aggregation form changes from (αβ)6 hexamer to (αβ)3 trimer to (αβ)monomer. After the dissociation of the original phycocyanin into dynamic equilibrium, the quantum yield of the mixture (the quantum of light energy absorbed and transmitted by phycocyanin in light energy transport in relation to fluorescence excitation, which is used to evaluate the denaturation of the purified phycocyanin) was reduced to 50% of that of the original mixture [33]. When dissolved in dilute phosphate buffer at low concentrations (<30 mmol/L), the (αβ) monomer dominates, and the loose structure allows the chromophore to exist in a high degree of conformational freedom, which reduces the fluorescence quantum yield based on its conjugated planes, leading to a decreasing absorbance of the system [12, 34], and a "bleaching" phenomenon is observed. This leads to a decreasing absorbance of the system [12, 34], resulting in a "bleaching" phenomenon.
Gustiningtyas et al. [35] introduced sodium tripolyphosphate to cross-link alginate with water-soluble chitosan (chitooligosaccharides) at pH 7 and screened the combination of alginate and chitooligosaccharides at a mass ratio of 3:4 to achieve the smallest particle size and the highest thermal stability, and the color remained unchanged even after holding the alginate at 50 °C for 90 min. Selig et al.[36] evaluated the effects of beet pectin, guar gum and soluble soybean polysaccharides on the thermal and hydrolytic stability of algal cyanobacterial proteins in protease treatment by combining them with polysaccharides to improve the color stability of algal cyanobacterial proteins. The combination of phycocyanin and polysaccharides was achieved under stirring conditions using citrate buffer. It was shown that beet pectin-stabilized phycocyanin particles had a large zeta potential, and the post-processing color difference value of ΔE was minimized in this system, resulting in better stability during heat and protease treatments.
On this basis, Zhang et al.[37] analyzed the ability of whey protein to improve the acid stability of phycocyanin by taking advantage of the fact that whey protein becomes transparent in pH 3 medium, and further evaluated the ability of α-lactalbumin, β-lactoglobulin, bovine serum albumin, immunoglobulin and glycomacropeptide among whey proteins to improve the heat stability of phycocyanin, and the results showed that natural and intact whey proteins provide the best protection for phycocyanin. The results showed that natural and intact whey proteins provide the best protection for phycocyanin and that the 3% phycocyanin system stabilized with 10% whey proteins has the potential to be used in acidic beverages, but the drawback is that it is not possible to improve the thermal stability of phycocyanin to the level of food industry production. At 80 °C, the brightness of the heat-stabilized phycocyanin decreased and the color began to change to green.
In addition, Zhang et al. [38] also used high hydrostatic pressure to promote the combination of alginate with whey protein and carrageenan, and showed that after high hydrostatic pressure treatment at 450 MPa and 600 MPa, the molecular structure and fluorescence properties of alginate-lactalbumin and alginate-carrageenan systems were changed, and the stabilization of the systems was improved in acidic to neutral media, and thermal stability was enhanced, and the storage stability of alginate was significantly improved under light. The storage stability of phycocyanin was significantly improved under light. It was further found that whey protein had the most significant color protection effect on the phycocyanin system when it was added to the same amount of phycocyanin at a mass fraction of 0.1%. After 5 d of direct sunlight in Ithaca in summer, the alginate dispersion with 0.1% whey protein retained the most blue hue [39].
In addition to binding to polysaccharides and proteins, sodium dodecyl sulfate micelles have been used to stabilize the blue color of phycocyanin [40]. Analysis of the stabilization mechanism showed that sodium dodecyl sulfate binds hydrophobically to the micelles and stabilizes the dominant helical structure of phycocyanin, thus stabilizing the unprotonated (blue) form of phycocyanin and preventing it from converting to the protonated (green) form at low pH.
However, sodium lauryl sulfate is not listed in the food additive use standards and the concentration of sodium lauryl sulfate required to form micelles imparts a detergent taste to the food, making it unacceptable to consumers. In a patent published by Marie et al [41], the delivery of phycocyanin is described using a water/oil/water triple emulsion structure, which maintains the relative stability of the pigment in the inner aqueous phase, but has the disadvantage that a large amount of encapsulation material is required, which results in a very low percentage of phycocyanin in the final product. In addition, the blue color delivery system does not have good transparency, which limits its application in water-based food products. Similarly, Batista et al [42] reported that phycocyanin and lutein were added to the aqueous and oily phases of oil-in-water emulsions, respectively, and that their stable dispersion and antioxidant properties were of great value in high-fat foods such as mayonnaise.
3.4 Application of algal blue protein in medical field
In addition to its health care functions, alginate has been widely used in the medical field because of its special properties. As shown in Table 4, in drug delivery to cancer cells, alginate can either be embedded and delivered into cancer cells to trigger apoptosis and autophagy through photodynamic therapy; it can also be combined with traditional anticancer drugs, such as cisplatin and magnetic particles, to enhance the degree of Fenton's reaction[72] , so as to kill the cancer cells; it can also be assembled to form a stable drug delivery carrier as a fluorescent protein, so as to make the nanoparticles stable in body fluid transport and not cause hemolysis, rejection and other reactions. It can also be used as a fluorescent protein to form a stable drug delivery carrier, so that the nanoparticles are stable and do not cause hemolysis and rejection in body fluids.
Al-Malki [73] used human serum albumin, the highest plasma albumin, to encapsulate phycocyanin, and this binary nanoparticle showed considerable antioxidant potential and free radical scavenging, and its anti-proliferative and pro-apoptotic abilities against hepatocellular carcinomas and breast cancers have been demonstrated in in vitro experiments. In addition, phycocyanin plays a key role in reaching the target organ and increasing the bioavailability of the nanoparticles.
Cheng et al [74] designed a biotin-chitooligosaccharide-dithiobispropionic acid structure modified by phycocyanin for the loading of curcumin. The above particles were bound to phycocyanin at 4 ℃, and the stable grafting of phycocyanin was achieved by the interactions of biotin with phycocyanin and the electrostatic interactions between positively charged chitooligosaccharides and negatively charged phycocyanin. Curcumin is located in the cavity formed by chitosan and phycocyanin. The disulfide bond formed between chitosan and curcumin endows this carrier with oxidation-reduction sensitivity, allowing the drug to be released in response to the high concentration of glutathione in the tumor cells, and it has the potential to achieve targeted transport to the tumor site.
In addition, phycocyanin, as a light-responsive protein, has been gradually explored for its great potential in optogenetic research. Since Deisseroth proposed the theory of "optogenetics" in 2006[75] , in the field of neuroscience, the microcurrent modulation of human cells through light-control technology has pointed out a feasible direction for solving the existing difficult problems[76] . There are few reports on the optogenetic studies involving phycocyanin, but Zhao et al. [7] initially explored it by preparing and incorporating gold nanoparticles with an average particle size of 5 nm into an amphiphilic polymer [77], and the gold nanoparticles encapsulated in the amphiphilic polymer were connected with phycocyanin in a mortise-and-tenon configuration through hydrophobic interactions, and this structure is similar to a mortise and tenon structure. The amphiphilic polymer-coated gold nanoparticles were connected to the phycocyanin through hydrophobic interactions in a "mortise-and-tenon" like manner, and this structure remained stable in agarose gel electrophoresis.
This study is conducive to combining the biocatalytic [78-79], nanosensing and biomedical functions of gold nanoparticles, such as labeling, imaging, tracing, and therapeutics [80-81], with the unique optical properties of phycocyanin. The synthesis of silver nanoparticles using phycocyanin is even easier, as phycocyanin transforms electrons from the ground state to the excited state under light conditions, and the electrons that undergo energy level jumps undergo a reduction reaction with silver nitrate (AgNO3) in the environment, resulting in the formation of phycocyanin-mediated silver nanoparticles [82]. The silver nanoparticles can take full advantage of their spectral antimicrobial activity against Gram-positive and Gram-negative bacteria, and their excellent antitumor properties have been verified by in vitro and in vivo experiments [83].
The application of phycobiliproteins to fluorescent probes has developed rapidly, and with the rapid development of the corresponding fluorescence activation and immunoassay fields, patents on the application of phycobiliproteins and alginyl cyanobacteria to fluorescent probes have been appearing continuously [33, 84]. However, the number of patents obtained for phycocyanin, as one of the phycobiliproteins, is much lower than that of the above two proteins under the same branch [17], because the stability of its application has not been fundamentally improved [85].
Nevertheless, to take advantage of the unique fluorescent properties of phycocyanin, it can also be used as a diagnostic probe by combining it with specific recognition elements (e.g., biotin, antibodies, and streptavidin) [43, 74]. Sun et al. [86] first stabilized the structure of the algalbumin (αβ) 3 trimer with formaldehyde to inhibit degradation at lower concentrations or under severe heating conditions, and then bound it to R-phycocyanin with glutaraldehyde, showing high energetic coupling and stability, which can be used as a fluorescent probe in immunoassays. Singh et al.[87] optimized the extraction of phycocyanin and investigated its potential for genomic DNA staining of erythrocytes, leukocytes, platelets, and lymphocytes at 25°C, and concluded that phycocyanin could be used as a partial substitute for ethidium bromide in immunological analyses and DNA staining. Zhao [88] attached alginate to gelatin nanoparticles embedded with Rhodobacter sphaeroides, in which alginate was adsorbed on the surface of the nanoparticles, and the energy transfer with Rhodobacter sphaeroides, which was not in direct contact with the nanoparticles, was dominated by dipole-dipole interaction. The system used phycocyanin as a reaction indicator to clarify the relationship between the photo-induced damage of B. burgdorferi and the production of oxygen radicals and oxygen supply.
4 Outlook
Phycocyanin is a scarce natural blue pigment in the food industry, and its potential application in the food industry should be fully utilized. In order to maintain the physiological activity of phycocyanin in the human body, the current research mainly focuses on the construction of nanoparticles for the delivery of phycocyanin in order to improve its bioavailability. However, there is a need for further development of delivery systems with good stability, high loading rate and slow release to expand the scope of application of phycocyanin in health food and even in pharmaceuticals.
This paper summarizes the ways to realize the homeostasis of phycocyanin and provides corresponding examples. At present, the biggest bottleneck in the practical application of phycocyanin lies in the maintenance of its structure and the stability of its color. Happily, new solutions and means for alginate homeostasis are constantly appearing, and it is believed that under the guidance of China's "Vision 2035", alginate, which is located in the key field of life and health, will have a broader space for development in time, and alginate will have a wider application in the field of foodstuffs due to its special color and functional activity. The algal blue protein will be more widely used in the food field with its special color and functional activity.
References
[1] ERIKSEN N T. Production of phycocyanin -a pig- ment with applications in biology , biotechnology, foods and medicine [J ]. Applied Microbiology and Biotechnology , 2008 , 80(1): 1-14.
[2] CHENTIR I , HAMDI M , LI S , et al. Stability, bio -functionality and bio -activity of crude phyco cyanin from a two - phase cultured Saharian Arthrospira sp. strain[J]. Algal Research , 2018 , 35: 395-406.
[3] Yu Li-Yan . Research progress on the properties and extraction technology of algal blue protein[J]. Fujian Light Textile , 2020(5): 46-51.
YU L Y. Advances in properties and extraction techniques of phycocyanin [J]. The Light & Textile Industries of Fujian , 2020(5): 46-51.
[4] PUZORJOV A , MCCORMICK A J. Phycobiliproteins from extreme environments and their potential appli- cations[J]. Journal of Experimental Botany , 2020 , 71
(13): 3827-3842.
[5] BÖCKER L , HOSTETTLER T , DIENER M , et al. Time -temperature -resolved functional and structural changes of phycocyanin extracted from Arthrospira platensis/Spirulina[ J ]. Food Chemistry , 2020 , 316: 126374.
[6] FERRARO G , IMBIMBO P , MARSEGLIA A , et al. X -ray structure of C -phycocyanin from Galdieria phlegrea: Determinants of thermostability and com- parison with a C -phycocyanin in the entire phyco- bilisome[J]. Biochimica et Biophysica Acta (BBA) - Bioenergetics , 2020 , 1861(9): 148236.
[7] ZHAO X , ZHAO X , YUAN M , et al. Study on physisorption between phycocyanin and gold nanoparticles[J]. Luminescence , 2019 , 34(6): 623- 627.
[8] TABARZAD M , ATABAKI V , HOSSEINABADI T. Anti -inflammatory activity of bioactive compounds from microalgae and cyanobacteria by focusing on the mechanisms of action [J]. Molecular Biology Re- ports , 2020 , 47 : 6193-6205.
[9] LIU Qi, LI Wenjun, TANG Zhihong, et al. Research progress on the role of algal cyanoproteins in the prevention and treatment of oxidative stress-related diseases[J]. Marine Science , 2017, 41(10): 132-138.
LIU Q , LI W J , TANG Z H , et al. Research ad- vances in the preventative and therapeutic effects of phycocyanin on oxidative stress -related diseases [J]. Marine Sciences , 2017 , 41(10): 132-138.
[10] Hao Shuai, Qin Yu, Wang Chengtao. Progress of Research on Physiological Activity of Functional Food Algae Cyanin [J]. Journal of Food and Biotechnology , 2017 , 36
(12): 1233-1240.
HAO S , QIN Y , WANG C T. Research progress of the physiological activity of functional food phyco- cyanin[J]. Journal of Food Science and Biotechnolo- gy , 2017 , 36(12): 1233-1240.
[11] PRABAKARAN G , SAMPATHKUMAR P , KAVISRI M , et al. Extraction and characterization of phyco- cyanin from Spirulina platensis and evaluation of its Extraction and characterization of phyco- cyanin from Spirulina platensis and evaluation of its anticancer , antidiabetic and antiinflammatory effect [J]. International Journal of Biological Macro- molecules , 2020 , 153 : 256-263.
[12] KUPKA M , SCHEER H. Unfolding of C -phyco- cyanin followed by loss of non -covalent chro- mophore -protein interactions [J]. Biochimica et Bio- physica Acta (BBA)-Bioenergetics , 2008 , 1777(1): 94-103.
[13] MA Y , XIE J , ZHANG C , et al. Three -stage re-folding/unfolding of the dual-color β-subunit in R - phycocyanin from Polysiphonia urceolata[J]. Biochem- ical and Biophysical Research Communications, 2007 , 352(3): 787-793.
[14] TONG X , PRASANNA G , ZHANG N , et al. Spec- troscopic and molecular docking studies on the in- teraction of phycocyanobilin with peptide moieties of C - phycocyanin [ J ]. Spectrochimica Acta Part A : Molecular and Biomolecular Spectroscopy , 2020, 236: 118316.
[15] NOURMOHAMMADI N , SOLEIMANIAN - ZAD S, SHEKARCHIZADEH H. Effect of Spirulina (Arthrospi- ra platensis) microencapsulated in alginate and whey protein concentrate addition on physicochemical and organoleptic properties of functional stirred yogurt[J]. Journal of the Science of Food and Agriculture, 2020 , 100(14): 1-9.
[16] DEV A , MOHANBHAI S J , KUSHWAHA A C , et al. κ -carrageenan -C -phycocyanin based smart in- jectable hydrogels for accelerated wound recovery and real - time monitoring [J ] . time monitoring [J ]. Acta Biomaterialia, 2020 , 109: 121-131.
[17] SEKAR S , CHANDRAMOHAN M. Phycobiliproteins as a commodity: Trends in applied research, patents and commercialization [J]. Journal of Applied Phycology , 2008 , 20(2): 113-136.
[18] MAZINANI S , FADAEI V , KHOSRAVI -DARANI K. Impact of Spirulina platensis on physicochemical properties and viability of Lactobacillus acidophilus of probiotic UF feta cheese: microalgal incorporation probiotic UF feta cheese[J]. Journal of Food Process- ing and Preservation , 2016 , 40(6): 1318-1324.
[19] MOHAMMADI -GOURAJI E , SOLEIMANIAN -ZAD S , GHIACI M. Phycocyanin-enriched yogurt and its antibacterial and physicochemical properties during
21 days of storage[J]. lwt , 2019 , 102 : 230-236.
[20] KAUR S , KHATTAR J I S , SINGH Y , et al. Ex- traction, purification and characterization of phyco- cyanin from Anabaena fertilissima PUPCCC 410.5: as a natural and food grade stable pigment [J]. Jour nal of Applied Phycology , 2019 , 31(3): 1685-1696.
/
[21] GALETOVIC A , SEURA F , GALLARDO V , et al. Use of phycobiliproteins from Atacama cyanobacteria as food colorants in a dairy beverage prototype [J]. Foods , 2020 , 9(2): 244-257.
[22] CAMPOS ASSUMPÇÃO DE AMARANTE M , CAV- ALCANTE BRAGA A R , SALA L , et al. Colour stability and antioxidant activity of C -phycocyanin - added ice creams after in vitro digestion [J] . Food Research International , 2020 , 137: 109602.
[23] JESPERSEN L , STRØMDAHL L D , OLSEN K , et al. Heat and light stability of three natural blue colorants for use in confectionery and beverages [J]. European Food Research and Technology , 2005, 220(3/4): 261-266.
[24] DEWI E N , KURNIASIH R A , PURNAMAYATI L. The application of microencapsulated phycocyanin as a blue natural colorant to the quality of jelly candy [C]/ /IOP Conference Series : Earth and Environmental Science. /IOP Conference Series : Earth and Environmental Science. Yogyakarta , INDONESIA : IOP Publishing Ltd , Dirac House , Temple Back , Bristol BS1 6BE. England , 2018 , 116 : 012047.
[25] FRADINHO P , NICCOLAI A , SOARES R , et al. Effect of Arthrospira platensis (Spirulina) incorpora- tion on the rheological and bioactive properties of gluten -free fresh pasta [J]. Algal Research , 2020, 45: 101743.
[26] BATISTA A P , NICCOLAI A , FRADINHO P , et al. Microalgae biomass as an alternative ingredient in cookies: sensory , physical and chemical proper- ties , antioxidant activity and in vitro digestibility [J]. antioxidant activity and in vitro digestibility [J]. Algal Research , 2017 , 26: 161-171.
[27] BATISTA A P , NICCOLAI A , BURSIC I , et al. Microalgae as functional ingredients in savory food products: application to wheat crackers [J]. foods, 2019 , 8(12): 611-633.
[28] NICCOLAI A , VENTURI M , GALLI V , et al. De- velopment of new microalgae-based sourdough "cros- tini": functional effects of Arthrospira platensis ( Spirulina) addition [J]. Scientific Reports , 2019 , 9
(1): 19433.
[29] BARKALLAH M , BEN ATITALLAH A , HENTATI F , et al. Effect of Spirulina platensis biomass with high polysaccharides content on quality attributes of common carp (Cyprinus carpio) and common barbel (Barbus barbus) fish burgers [J]. Applied Sciences, 2019 , 9(11): 2197.
[30] NICCOLAI A , SHANNON E , ABU-GHANNAM N , et al. Lactic acid fermentation of Arthrospira platen- sis (Spirulina) biomass for probiotic-based products
[J]. Journal of Applied Phycology , 2019 , 31(2):
1077-1083.
[31] XU Chunming, LI Ting, WANG Yingying, et al. Progress of research on edible blue pigment and its use[J]. China Food Additives , 2014(1): 208- 214.
XU C M , LI T , WANG Y Y , et al. Research progress of edible blue pigments and its application status[J]. China Food Additives , 2014(1): 208-214.
[32] National Health and Family Planning Commission of the People's Republic of China. National Standard for Food Safety: Standard for the Use of Food Additives: GB 2760 - 2014 [S]. Beijing: China Standard Press, 2014.
National Health and Family Planning Committee of China. national food safety standard for food addi- tive use: GB 2760-2014[S]. Beijing: Standards Press of China , 2014.
[33] KUDDUS M , SINGH P , THOMAS G , et al. Recent developments in production and biotechnological ap- plications of C-phycocyanin[J]. BioMed Research In- ternational , 2013 , 2013 : 742859.
[34] THOREN K L , CONNELL K B , ROBINSON T E , et al. The free energy of dissociation of oligomeric structure in phycocyanin is not linear with denatu- rant[J]. Biochemistry , 2006 , 45: 12050-12059.
[35] GUSTININGTYAS A , SETYANINGSIH I , HAR- DININGTYAS S D , et al. Improved stability of phycocyanin from Spirulina platensis encapsulated by water-soluble chitosan nanoparticles [C]//IOP Confer- ence Series: Earth and Environmental Science. soluble chitosan nanoparticles [C]//IOP Confer- ence Series: Earth and Environmental Science. Penang, Malaysia. The World Seafood Congress
2019 - "Seafood Supply Chains of the Future: In- novation , Responsibility , Sustainability". 2020 , 414: 012005.
[36] SELIG M J , MALCHIONE N M , GAMALELDIN S, et al. Protection of blue color in a spirulina derived phycocyanin extract from proteolytic and thermal degradation via complexation with beet -pectin [J]. Food Hydrocolloids , 2018 , 74 : 46-52.
[37] ZHANG Z , LI Y , ABBASPOURRAD A. Improve- ment of the colloidal stability of phycocyanin in acidified conditions using whey protein -phycocyanin interactions [ J ]. Food Hydrocolloids , 2020 , 105: 105747.
[38] ZHANG Z , CHO S , DADMOHAMMADI Y , et al. Improvement of the storage stability of C -phyco- cyanin in beverages by high -pressure processing [J]. Food Hydrocolloids , 2021 , 110: 106055.
[J]. Journal of Applied Phycology , 2019 , 31(2):
1077-1083.
[31] XU Chunming, LI Ting, WANG Yingying, et al. Progress of research on edible blue pigment and its use[J]. China Food Additives , 2014(1): 208- 214.
XU C M , LI T , WANG Y Y , et al. Research progress of edible blue pigments and its application status[J]. China Food Additives , 2014(1): 208-214.
[32] National Health and Family Planning Commission of the People's Republic of China. National Standard for Food Safety: Standard for the Use of Food Additives: GB 2760 - 2014 [S]. Beijing: China Standard Press, 2014.
National Health and Family Planning Committee of China. national food safety standard for food addi- tive use: GB 2760-2014[S]. Beijing: Standards Press of China , 2014.
[33] KUDDUS M , SINGH P , THOMAS G , et al. Recent developments in production and biotechnological ap- plications of C-phycocyanin[J]. BioMed Research In- ternational , 2013 , 2013 : 742859.
[34] THOREN K L , CONNELL K B , ROBINSON T E , et al. The free energy of dissociation of oligomeric structure in phycocyanin is not linear with denatu- rant[J]. Biochemistry , 2006 , 45: 12050-12059.
[35] GUSTININGTYAS A , SETYANINGSIH I , HAR- DININGTYAS S D , et al. Improved stability of phycocyanin from Spirulina platensis encapsulated by water-soluble chitosan nanoparticles [C]//IOP Confer- ence Series: Earth and Environmental Science. soluble chitosan nanoparticles [C]//IOP Confer- ence Series: Earth and Environmental Science. Penang, Malaysia. The World Seafood Congress
2019 - "Seafood Supply Chains of the Future: In- novation , Responsibility , Sustainability". 2020 , 414: 012005.
[36] SELIG M J , MALCHIONE N M , GAMALELDIN S, et al. Protection of blue color in a spirulina derived phycocyanin extract from proteolytic and thermal degradation via complexation with beet -pectin [J]. Food Hydrocolloids , 2018 , 74 : 46-52.
[37] ZHANG Z , LI Y , ABBASPOURRAD A. Improve- ment of the colloidal stability of phycocyanin in acidified conditions using whey protein -phycocyanin interactions [ J ]. Food Hydrocolloids , 2020 , 105: 105747.
[38] ZHANG Z , CHO S , DADMOHAMMADI Y , et al. Improvement of the storage stability of C -phyco- cyanin in beverages by high -pressure processing [J]. Food Hydrocolloids , 2021 , 110: 106055.
评论
发表评论