Method for synthesizing ascorbyl glucoside by transforming yeast lysate and use thereof

Abstract

This invention relates to a method for synthesizing ascorbate glucoside via yeast lysate and its application, belonging to the field of cosmetic technology. The invention discloses a Bifida ferment lysate, which is a fermentation product lysate of *Bifidobacterium longum*, wherein the *Bifidobacterium longum* is at least one of *Bifidobacterium longum* HJ-005, *Bifidobacterium longum* subsp. *CGMCC* 1.2186, and *Bifidobacterium longum* subsp. *infant* CGMCC 1.15639; the nucleotide sequence of the 16S rRNA of *Bifidobacterium longum* HJ-005 is shown in SEQ ID NO: 1. This invention uses a specific fermentation product lysate of *Bifidobacterium longum* to catalyze the transglycosylation reaction of vitamin C, obtaining a reaction product containing AA2G, thereby increasing the yield of AA2G, significantly reducing the preparation cost of AA2G, and significantly inhibiting the production of melanin in zebrafish embryos, exhibiting a whitening effect. It can be used as a cosmetic raw material without purification.

Description

Technical Field

[0001] This invention relates to the field of skincare technology, and in particular to a method for synthesizing ascorbate glucoside through the conversion of yeast lysate and its application. Background Technology

[0002] Vitamin C (ascorbic acid, AA) is an important water-soluble antioxidant widely used in cosmetics and health products, possessing antioxidant, collagen-promoting, whitening (inhibiting tyrosinase), anti-inflammatory, and repairing effects. However, it also has drawbacks, primarily including: extreme chemical instability, making it highly susceptible to oxidative degradation (affected by light, heat, pH, and oxygen), leading to formula failure or reduced efficacy. AA2G (Ascorbic Acid 2-Glucoside) is a glucoside derivative of vitamin C, formed by the combination of vitamin C and glucose via a glycosidic bond. Its advantages include: higher stability: less prone to oxidation, allowing for long-term preservation in formulations; preservation of biological activity: hydrolyzed by enzymes (such as α-glucosidase) in the skin or body, slowly releasing active vitamin C to exert its effects; and better gentleness: less irritating to the skin than high concentrations of the original vitamin C. Therefore, AA2G is currently one of the most commonly used and stable vitamin C derivatives in high-end skincare products (widely used by many cosmetic brands).

[0003] Currently, AA2G is mainly produced through chemical enzymatic synthesis or biotransformation. The mainstream processes are as follows: (1) Enzymatic synthesis (non-fermentation method), which is the mainstream industrial method. AA (vitamin C) + glucose are catalyzed by specific glycosyltransferases (such as UDP-glycosyltransferase or glycosyltransferases derived from microorganisms / plants) to produce AA2G. The enzymes in this reaction system need to be purified. (2) AA2G is catalyzed by expressing specific glycosyltransferases through genetically engineered bacteria. The resulting AA2G needs to be separated and purified, and its composition is relatively high.

[0004] Bifida ferment lysate is a physiological lysate obtained from Bifidobacterium through fermentation and subsequent treatment. In vitro experiments have shown that the fermentation product obtained after a series of operations including culturing and inactivation of Bifidobacterium possesses numerous effects such as anti-oxidation, anti-aging, and barrier repair, showing great promise in improving the skin's microecological environment. Furthermore, it is already included in the "Catalogue of Used Cosmetic Raw Materials," highlighting the potential and importance of Bifida ferment lysate in the skincare market. However, there are currently no reports on the direct biotransformation of AA2G using microbial lysates (containing thousands of biomolecules), nor on the synthesis of AA2G using Bifidobacterium longum. Summary of the Invention

[0005] The purpose of this invention is to overcome the shortcomings of the prior art and provide a method for synthesizing ascorbate glucoside by converting yeast lysate and its application.

[0006] To achieve the above objectives, the technical solution adopted by the present invention is as follows: In a first aspect, the present invention provides a Bifida ferment lysate, which is a fermentation product lysate of Bifidobacterium longum, wherein the Bifidobacterium longum is at least one of Bifidobacterium longum HJ-005, Bifidobacterium longum subsp. CGMCC 1.2186, and Bifidobacterium longum subsp. infantum CGMCC 1.15639; the nucleotide sequence of the 16S rRNA of Bifidobacterium longum HJ-005 is shown in SEQ ID NO: 1.

[0007] This invention obtains lysate by fermentation with different Bifidobacterium longum, which can catalyze the transglycosylation reaction of vitamin C to obtain ascorbic acid-2-glucoside, thereby increasing the yield of ascorbic acid-2-glucoside and showing better results than other lactic acid bacteria.

[0008] Secondly, the present invention provides a method for preparing the Bifida Fermentata lysate, wherein the Bifida Fermentata is homogenized under high pressure to break the cell wall, and the cell supernatant is obtained by solid-liquid separation, which is the Bifida Fermentata lysate.

[0009] Furthermore, the pressure for high-pressure homogenization is preferably 800~1500 bar, for example, including but not limited to any point value or any range of two points from 800, 900, 1000, 1100, 1200, 1300, 1400 and 1500 bar.

[0010] Furthermore, the solid-liquid separation method includes centrifugation, with centrifugation conditions of 10,000 to 15,000 rpm for 10 to 20 minutes, preferably 12,000 rpm for 15 minutes.

[0011] Furthermore, a preservative is added to the bifida lysate to achieve a preservative effect. Preferably, the preservative is at least one of 1,2-hexanediol, pentanediol, and hydroxyacetophenone.

[0012] Furthermore, the final volume concentration of 1,2-hexanediol is preferably 0.1% to 1%, for example, including but not limited to any point value or any range of two points such as 0.1%, 0.3%, 0.5%, 0.8% and 1%.

[0013] Furthermore, the final volume concentration of pentanediol is preferably 0.1% to 1%, for example, including but not limited to any point value or any range of two points such as 0.1%, 0.3%, 0.5%, 0.8% and 1%.

[0014] Furthermore, the final volume concentration of hydroxyacetophenone is preferably 0.1% to 1%, for example, including but not limited to any point value or any range of two points such as 0.1%, 0.3%, 0.5%, 0.8% and 1%.

[0015] Thirdly, the present invention provides the application of the bifida lysate in the preparation of ascorbic acid-2-glucoside.

[0016] Fourthly, the present invention provides a method for preparing ascorbic acid-2-glucoside, wherein the Bifida ferment lysate is used to catalyze the transglycosylation reaction of vitamin C to obtain ascorbic acid-2-glucoside.

[0017] Further, maltose, vitamin C, disodium hydrogen phosphate and the Bifida ferment lysate were mixed, the pH was adjusted to 3.0-8.0, and the mixture was incubated at 35-45°C in the dark for 2-6 hours. The reaction was terminated by high-temperature treatment at 90-100°C to obtain the reaction product containing ascorbic acid-2-glucoside.

[0018] Furthermore, the volume concentration of the bifida lysate is preferably 5% to 20%, for example, including but not limited to any point value or any range of two points such as 5%, 8%, 10%, 15%, 18% and 20%.

[0019] Furthermore, the maltose concentration is preferably 50-600 mM, for example, including but not limited to any point value or any range of two points from 50, 100, 150, 200, 250, 300, 350, 400, 450, 500, 550, and 600 mM; the vitamin C concentration is preferably 20-260 mM, for example, including but not limited to any point value or any range of two points from 20, 40, 60, 80, 100, 120, 140, 160, 180, 200, 220, 240, and 260 mM; the disodium hydrogen phosphate concentration is preferably 20-260 mM, for example, including but not limited to 20, 40, 60, 80, 100, 120, 140, 160, 180, 200, 220, 240, and 260 mM. The pH value is any point value or a range of any two points from mM, etc.; the pH value is preferably 3.0 to 8.0, for example, including but not limited to any point value or a range of any two points from 3.2, 3.4, 3.6, 3.8, 4.0, 4.2, 4.4, 4.6, 4.8, 5.0, 5.2, 5.4, 5.6, 5.8, 6.0, 6.2, 6.4, 6.6, 6.8, 7.0, 7.2, 7.4, 7.6, 7.8 and 8.0.

[0020] Furthermore, the pH value can be adjusted by using a citric acid solution, wherein the concentration of the citric acid is preferably 10~150 mM, for example, including but not limited to any point value or any range of any two points from 10, 20, 30, 40, 50, 60, 70, 80, 90, 100, 110, 120, 130, 140, 150 mM.

[0021] Furthermore, the incubation temperature in the dark includes, but is not limited to, any point value or any range of two points from 35, 37, 38, 40, 42 and 45°C.

[0022] Furthermore, the incubation time in the dark includes, but is not limited to, any point value or any range of two points such as 2, 3, 4, 5 and 6 hours.

[0023] Furthermore, the high-temperature processing temperature includes, but is not limited to, any point value or any range of two points among 90, 92, 95, 98 and 100℃.

[0024] In a specific embodiment of the present invention, the reaction is terminated by a water bath at 100°C for 8 to 15 minutes. The water bath time includes, but is not limited to, any point value or any range of two points such as 8, 9, 10, 12 and 15 minutes.

[0025] Fifthly, the present invention provides a Bifidobacterium longum, wherein the Bifidobacterium longum is Bifidobacterium longum HJ-005, and the nucleotide sequence of its 16S rRNA is shown in SEQ ID NO: 1.

[0026] In a sixth aspect, the present invention provides a reaction product containing ascorbic acid-2-glucoside, which is prepared by the method described above.

[0027] In a seventh aspect, the present invention provides the application of the reaction product containing ascorbic acid-2-glucoside in the preparation of skin whitening products.

[0028] Eighthly, the present invention provides a cosmetic product containing the aforementioned reaction product containing ascorbic acid-2-glucoside.

[0029] Compared with the prior art, the beneficial effects of the present invention are as follows: This invention utilizes the lysates of specific *Bifidobacterium longum* (HJ-005, *Bifidobacterium longum* subsp. *CGMCC* 1.2186, and *Bifidobacterium longum* subsp. *infant* CGMCC 1.15639) to catalyze the transglycosylation reaction of vitamin C under specific conditions, thereby obtaining a reaction product containing AA2G. This increases the yield of AA2G, significantly reduces the preparation cost of AA2G, and can significantly inhibit the production of melanin in zebrafish embryos, thus having a whitening effect. It can be used as a cosmetic raw material without purification. Attached Figure Description

[0030] Figure 1 Phylogenetic tree of Bifidobacterium longum HJ-005.

[0031] Figure 2 The results of Gram staining of Bifidobacterium longum HJ-005 are shown in the microscopic examination.

[0032] Figure 3 This is the HPLC chromatogram of AA2G standard.

[0033] Figure 4 This is an HPLC chromatogram of the transformation products of Bifidobacterium longum HJ-005 lysate.

[0034] Figure 5 This is an HPLC chromatogram of the transformation products of lysate from Bifidobacterium longum subsp. longum (CGMCC 1.2186).

[0035] Figure 6 This is an HPLC chromatogram of the transformation products of lysate from Bifidobacterium longum subsp. infantis (CGMCC 1.15639).

[0036] Figure 7 The content of AA2G in the transformation products of Bifidobacterium HJ-005 lysate at different time intervals.

[0037] Figure 8 A bar chart showing melanin inhibition in zebrafish.

[0038] Figure 9 This is a representative graph showing the whitening efficacy test results. A represents the blank control group; B represents the positive control group; C represents the sample treatment group; and D represents the model group. Detailed Implementation

[0039] To better illustrate the purpose, technical solution, and advantages of this invention, the invention will be further described below with reference to specific embodiments. Unless otherwise specified, other materials and reagents used in the embodiments are commercially available.

[0040] Example 1: Screening and Identification of Fermentation Strains 1. Isolation and Purification: Samples from the intestinal contents (feces) of healthy individuals and traditional fermented food (pickled vegetables) were collected. Modified MRS and M17 media were used, with separate culture conditions set for different bacterial strains, followed by serial dilutions and streaking. The cultures were incubated at 37°C, and single colonies were picked for repeated purification to obtain pure cultures. Specifically, *Lactobacillus*, *Bifidobacterium*, and *Leuconostoc* strains were cultured on modified MRS medium, with *Lactobacillus* and *Bifidobacterium* requiring anaerobic incubation for 48–72 h; *Lactococcus* and *Streptococcus* strains were cultured on M17 medium under aerobic or microaerobic conditions for 24–48 h.

[0041] The modified MRS medium (per liter) contains: 10.0 g peptone, 10.0 g beef extract, 4.0 g yeast extract, 20.0 g glucose, 1.0 g Tween 80, 2.0 g K2HPO4·3H2O, 5.0 g sodium acetate trihydrate, 2.0 g triammonium citrate, 0.2 g MgSO4·7H2O, 0.05 g MnSO4·4H2O, and 0.5 g L-cysteine, adjusted to pH 6.2±0.1.

[0042] M17 medium (per liter) contains: 5.0 g peptone, 5.0 g soybean peptone, 2.5 g beef extract, 2.5 g yeast extract, 5.0 g glucose, 5.0 g lactose, 0.5 g ascorbic acid, 0.25 g MgSO4·7H2O, 2.5 g K2HPO4, and pH adjusted to 6.8±0.1.

[0043] 2. Identification: Gram staining, microscopic examination and basic physiological and biochemical tests were performed on the pure cultures obtained in step 1. The physiological and biochemical characteristics of different strains were different.

[0044] Lactobacillus, Bifidobacterium, Lactococcus, and Streptococcus are all catalase-negative. Lactobacillus ferments glucose to produce lactic acid without producing gas. Bifidobacterium ferments glucose to produce lactic acid and acetic acid (molar ratio 2:3). Lactococcus ferments glucose to produce lactic acid without producing gas. Some strains of Streptococcus are hemolytic.

[0045] Following the method described in the literature (Xu Chao, Zhang Shaobing, Meng Jun, et al. Preliminary study on antioxidant activity and cholesterol degradation capacity of different lactic acid bacteria [J]. Food and Fermentation Industries, 2023, 49(02):152-158+165.DOI:10.13995 / j.cnki.11-1802 / ts.031305.), the antioxidant capacity of pure cultures with potential probiotic functions was compared, and strains with strong antioxidant capacity were obtained.

[0046] Genomic DNA was further extracted from each lactic acid bacteria strain, and PCR amplification was performed using universal primers for the 16S rRNA gene. The primer sequences were: upstream primer 27F (5'-AGAGTTTGATCMTGGCTCAG-3') and downstream primer 1492R (5'-TACGGYTACCTTGTTACGACTT-3'). The amplification system (25 μL) consisted of: 2.5 μL of 10×PCR Buffer, 2 μL of dNTPs mixture (2.5 mmol / L), 0.5 μL each of upstream and downstream primers (10 μmol / L), 0.2 μL of Taq DNA polymerase (5 U / μL), 1 μL of template DNA, and sterile double-distilled water to a total amplification volume of 25 μL. The amplification program was as follows: 94℃ pre-denaturation for 5 min; 94℃ denaturation for 30 s, 55℃ annealing for 30 s, 72℃ extension for 1.5 min, for a total of 35 cycles; 72℃ final extension for 10 min, and incubation at 4℃. After sequencing the amplified products, the obtained sequences were compared with the NCBI database to classify and identify the selected strains.

[0047] Bifidobacterium longum was finally screened from the feces. Bifidobacterium longum Streptococcus thermophilus was screened from kimchi. Streptococcus thermophilus Lactobacillus plantarum ( Lactiplantibacillus plantarum ) and lactococci ( Lactococcus sp.).

[0048]

[0049] Its and Bifidobacterium longum subsp. longum The ATCC 15707 strain showed high homology; comparison results from the NCBI Blast database showed a similarity of over 95%, and the phylogenetic tree is as follows. Figure 1 As shown, the microscopic results of Gram staining are as follows: Figure 2 As shown. The obtained Bifidobacterium longum (also known as Bifida ferment lysate) was named Bifidobacterium longum (as shown). Bifidobacterium longum HJ-005 was deposited at the China Center for Type Culture Collection (CCTCC) on July 23, 2025, with accession number CCTCC NO: M 20251676, at Wuhan University, China.

[0050] The obtained thermophilic streptococcus was named thermophilic streptococcus ( Streptococcus thermophilus HJA09, the obtained Lactobacillus plantarum was named Lactobacillus plantarum ( Lactiplantibacillus plantarum HJB73, the obtained lactococcus was named Lactococcus lactis ( Lactococcus sp.)HJG02.

[0051] Example 2 I. Experimental Methods 1. *Bifidobacterium longum* HJ-005, *Bifidobacterium longum* subsp. *longum* (CGMCC 1.2186), *Bifidobacterium longum* subsp. *infantum* (CGMCC 1.15639), *Streptococcus thermophilus* HJA09, *Lactobacillus plantarum* HJB73, and *Lactococcus lactis* HJG02 were inoculated into their respective slant agar media (modified MRS medium), anaerobically cultured at 37°C for 24 h, and continuously activated for two generations to obtain viable strains. Subsequently, single colonies of each strain were inoculated into 50 mL of the corresponding modified MRS liquid medium and anaerobically shaken at 37°C and 120 r / min for 18–20 h until the OD of the bacterial culture was reached. 600 The pH value reached 8.0, yielding the seed culture. Seed cultures of each strain were inoculated into fermenters with a 70% volume inoculum rate of 5% (volume concentration). Modified MRS medium was used, and fermentation was carried out under anaerobic conditions at 37℃ and 100 r / min for 24 h. During the process, 20% (volume concentration) ammonia was used to maintain the pH at 6.0–6.5. The OD value of the bacterial culture was measured. 600 The fermentation endpoint was reached when the cell count stopped increasing, yielding the fermentation broth. The fermentation broth was centrifuged at 4℃ and 10000 r / min for 20 min, and the cell pellet was collected. The pellet was washed twice with ultrapure water and resuspended in an equal volume of ultrapure water. The pellet was then subjected to high-pressure homogenization at 1000 bar twice to disrupt the cell walls. After homogenization, the pellet was centrifuged at 12000 rpm for 15 min to obtain the supernatant, which was used to prepare the lysate.

[0052] 2. Glycosylation reaction: A 100 L reaction system was constructed containing 500 mM maltose, 200 mM vitamin C, 200 mM disodium hydrogen phosphate, and 10% (final volume concentration) of lysate. The pH was adjusted to 5.2 with 100 mM citric acid. The mixture was incubated in the dark at 40 °C for 6 h and then stopped in a water bath at 100 °C for 10 min to obtain the reaction solution (lysate conversion product).

[0053] 3. Take 1 mL of the reaction solution and dilute it 10 times to obtain a diluted solution. Mix 250 μL of the diluted solution with 750 μL of acetonitrile, let it stand for 16 h, centrifuge at 12000×g for 10 min, collect the supernatant, and perform HPLC analysis. HPLC detection method: Agilent 1200 liquid chromatograph, using an Alltima 5 μm C18 (250×4.6 mm) column, isocratic elution with pure methanol and 0.02 mol / L potassium dihydrogen phosphate as the mobile phase at 30℃ and a flow rate of 0.8 mL / min, injection volume 10 μL, detection wavelength 210 nm, single run time 20 min.

[0054] II. Experimental Results Bifida ferment lysate contains α-amylase family glycosyl hydrolases that catalyze the reaction of vitamin C and maltose to produce AA2G. AA2G standard ( Figure 3 The retention time of the product was 7.872 min, and the transformation product of Bifidobacterium longum HJ-005 Bifida ferment lysate ( Figure 4 The retention time of AA2G was 7.984 min, with a difference of 1.42% between the two, within the 2.5% error range. Quantitative analysis using the internal standard method further confirmed that the transformation product was AA2G. (Bifidobacterium longum subsp. longum) Figure 5 ) and Bifidobacterium longum infantis subspecies ( Figure 6 The retention times of the lysate transformation products were 7.932 min and 7.929 min, respectively, with a difference of 0.76% and 0.72%, both within the error range of 2.5%. Further quantitative analysis using the internal standard method confirmed that the transformation product was AA2G.

[0055] The standard contained 0.1 g / L of AA2G. After approximately 10 minutes of reaction, the AA2G concentration in the lysate transformation products of *Bifidobacterium longum* HJ-005 was 0.85 g / L, the concentration in the lysate transformation products of *Bifidobacterium longum* subsp. *longum* was 0.81 g / L, and the concentration in the lysate transformation products of *Bifidobacterium longum* subsp. *infantum* was 0.78 g / L. No AA2G was generated in the lysate transformation products prepared by fermentation of *Streptococcus thermophilus* HJA09, *Lactobacillus plantarum* HJB73, and *Lactococcus lactis* HJG02.

[0056] The content of AA2G in the transformation products of lysates obtained at different times is as follows: Figure 7 As shown, AA2G can be prepared using Bifidobacterium longum HJ-005 lysate on a catalytic scale of 100 L, with a synthesis amount reaching 6.6 g / L in 3 h.

[0057] Example 3: Effects of different conditions on the conversion of Bifida ferment lysate into AA2G I. Experimental Methods (1) Maltose concentration: The maltose concentration was set to 50~600 mM, with a gradient of 50 mM. Other conditions remained unchanged, and the transglycosylation reaction was carried out according to the method in Example 2.

[0058] (2) Vitamin C concentration: The vitamin C concentration was set to 20~260 mM, with a gradient of 20 mM. Other conditions remained unchanged, and the transglycosylation reaction was carried out according to the method in Example 2.

[0059] (3) Effect of metal ions: In the transglycosylation reaction system, the disodium hydrogen phosphate in the original system was replaced with an equimolar metal salt, and lithium chloride (LiCl), sodium chloride (NaCl), magnesium chloride (MgCl2·6H2O), aluminum chloride (AlCl3·6H2O), potassium chloride (KCl), calcium chloride (CaCl2), manganese chloride (MnCl2·4H2O), ferrous chloride (FeCl2·4H2O), cobalt chloride (CoCl2·6H2O), copper chloride (CuCl2·2H2O) or zinc chloride (ZnCl2) were added respectively; other reaction conditions remained unchanged, and the transglycosylation reaction was carried out according to the method of Example 2.

[0060] (4) Effect of pH: The pH was set to 3.0~8.0, with a gradient of 0.2. The pH was adjusted with 100 mM citric acid, and other conditions remained unchanged. The transglycosylation reaction was carried out according to the method in Example 2.

[0061] II. Experimental Results The results showed that the lysate had the strongest ability to convert to AA2G at a maltose concentration of 500 mM; the AA2G content was highest at a vitamin C concentration of 200 mM; and the addition of metal ions had no significant effect on the conversion of Bifida ferment lysate to AA2G. The highest AA2G content was generated at pH 4.8–5.2.

[0062] In the optimal reaction mixture, with maltose concentration of 500 mM, vitamin C concentration of 200 mM, disodium hydrogen phosphate concentration of 200 mM, Bifida ferment lysate volume concentration of 10%, and pH adjusted to 5.2 with 100 mM citric acid, the maximum AA2G production was 6.6 g / L after reaction at 40°C in the dark for 3 h.

[0063] Example 4: Efficacy Test of Transformation Products of Bifidobacterium longum HJ-005 Lysate I. Experimental Methods Skin whitening effect (zebrafish embryo melanin inhibition test) Twenty 8-hour-old zebrafish embryos were exposed to a sample solution (sample treatment group). The sample solution was prepared by centrifugation and filtration of the lysate conversion product, followed by dilution to a volume concentration of 5% with fish embryo culture medium (prepared by dissolving 2940 mg anhydrous calcium chloride, 1233 mg magnesium sulfate heptahydrate, 630 mg sodium bicarbonate, and 55 mg potassium chloride in 10 L of water; pH 6.5–8.5; all chemicals were analytical grade). A blank control group (fish embryo culture medium), a 100% melanin inhibition model group (30 mg / L phenylthiourea), and a positive control group (2.5 g / L kojic acid) were also set up. After 48 hours of exposure, the fish embryos were photographed under a microscope to measure the melanin signal intensity and perform statistical analysis.

[0064] II. Experimental Results like Figure 8 , Figure 9 A, Figure 9 B Figure 9 C and Figure 9 As shown in D, the inhibition rate of melanin in zebrafish embryos by the sample treatment group was 12.19% ( p =0.00039), which significantly inhibited melanin production in zebrafish embryos, exhibiting a whitening effect. The whitening effect was not significant in the blank control group (0% melanin inhibition rate). The whitening effect was significant in the positive control group (30% melanin inhibition rate). The whitening effect was significant in the model control group (100% melanin inhibition rate).

[0065] Finally, it should be noted that the above embodiments are only used to illustrate the technical solutions of the present invention and are not intended to limit the scope of protection of the present invention. Although the present invention has been described in detail with reference to preferred embodiments, those skilled in the art should understand that modifications or equivalent substitutions can be made to the technical solutions of the present invention without departing from the essence and scope of the technical solutions of the present invention.

Claims

1. A Bifida ferment lysate, characterized in that, The product is a fermentation lysate of Bifidobacterium longum, wherein the Bifidobacterium longum is at least one of Bifidobacterium longum HJ-005, Bifidobacterium longum subsp. CGMCC 1.2186, and Bifidobacterium longum subsp. infantum CGMCC 1.15639; the nucleotide sequence of the 16S rRNA of Bifidobacterium longum HJ-005 is shown in SEQ ID NO:

1.

2. The method for preparing Bifida ferment lysate according to claim 1, characterized in that, The cell wall of Bifidobacterium longum as described in claim 1 is homogenized under high pressure, and the cell supernatant is obtained by solid-liquid separation, which is the Bifida Ferment Lysate.

3. The use of the Bifida Ferment Lysate of claim 1 in the preparation of ascorbic acid-2-glucoside.

4. A method for preparing ascorbic acid-2-glucoside, characterized in that, The Bifida Ferment Lysate of claim 1 was used to catalyze the transglycosylation of vitamin C to obtain ascorbic acid-2-glucoside.

5. The method as described in claim 4, characterized in that, Maltose, vitamin C, disodium hydrogen phosphate, and the Bifida ferment lysate as described in claim 1 are mixed, the pH is adjusted to 3.0-8.0, and the mixture is incubated at 35-45°C in the dark for 2-6 h. The reaction is terminated by high-temperature treatment at 90-100°C to obtain a reaction product containing ascorbic acid-2-glucoside.

6. The method as described in claim 5, characterized in that, The volume concentration of the Bifida Ferment Lysate is 5% to 20%.

7. A type of Bifidobacterium longum, characterized in that, The Bifidobacterium longum is Bifidobacterium longum HJ-005, and its 16S rRNA nucleotide sequence is shown in SEQ ID NO:

1.

8. A reaction product containing ascorbic acid-2-glucoside, characterized in that, It is prepared by the method described in any one of claims 4 to 6.

9. The use of the reaction product containing ascorbic acid-2-glucoside as described in claim 8 in the preparation of skin whitening products.

10. A cosmetic product, characterized in that, The cosmetic contains the reaction product containing ascorbic acid-2-glucoside as described in claim 8.

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