Views: 0 Author: Site Editor Publish Time: 2024-05-24 Origin: Site
Arbutin is a tyrosinase inhibitor, mainly blocks the synthesis of dopa and dopaquinone, curbing the production of melanin, thus with skin whitening effect. In the 1990s, it was first launched in Japan as a cosmetics whitener, following another whitening agent such as γ-cysteine and curvature acid. Not only on freckles, senile spots, chloasma has a fade effect, but also on the skin moisturizing, skin burns after the healing and acne is also quite effective. At present, the whitening and skin care market in developed countries has been almost monopolized by Arbutin.
β-Arbutin is obtained by chemical synthesis, while α-Arbutin only can be prepared by enzyme synthesis(microbial fermentation). In addition to the process difference, α-Arbutin is more likely to be soluble in water and have high temperature resistance, good optical stability, no cytotoxicity in a safe dose, and the effect of inhibiting melanin production is 10 times stronger than β-Arbutin, so α-Arbutin is generally used for advanced whitening cosmetics.
1. Stability
β-Arbutin and α-Arbutin are both derivatives of hydroquinone and will decompose into hydroquinone under certain conditions, and hydroquinone is a prohibited substance in cosmetics, so it is particularly necessary to ensure the stability of Arbutin applied to whitening products.
β-Arbutin decomposes above 50 ℃ to produce hydroquinone, and also produces hydroquinone under strong acid and strong alkali conditions. In addition, β-Arbutin can be hydrolyzed into hydroquinone by human epidermal microorganisms and β-glucosinase, and the acidic environment and artificial sweat can promote the hydrolysis of β-glucosinase on β- Arbutin, in which artificial sweat is more promoted. Therefore, attention should be paid to avoid these adverse factors, so as to ensure the safety and effectiveness of the use.
In the basic environment of cosmetics, temperature has little impact on the stability of α-Arbutin, when the temperature reaches about 100 ℃, Hydroquinone was still not detected in the α-Arbutin solution; Under pH = 5.2 and pH = 8.0 conditions, Hydroquinone was also not detected in α-Arbutin solution. However, under the conditions of pH = 1.0 and pH = 13.0, Hydroquinone detected in α-Arbutin solution; After save 72h under light avoidance conditions, No hydroquinone was detected in the α-Arbutin solution, Hydroquinone was detected in the α-Arbutin solution saved under exposure conditions, Meanwhile, the same Under UV exposure conditions, Hydroquinone was detected in α-Arbutin. Therefore, in the development and application of a series of products containing α-Arbutin, attention should be paid to avoid the strong acid and alkali environment and ultraviolet radiation.
From the above analysis, α-Arbutin is more stable than β-Arbutin.
2. Effectiveness
Some scholars have compared the effects of α-and β- Arbutin on their activity from mushrooms and mouse melanoma. The results show that β- Arbutin suppresses Tyrosinase from mushrooms and melanoma in mice by noncompetitive inhibition, while α-Arbutin only suppresses tyrosase from melanoma, and its mechanism is speculated as mixed inhibition. The inhibitory intensity of α- Arbutin is 10 times that of β- Arbutin.
3. Security
Some other scholars studied the inhibition of two compounds on melanin synthesis with cultured B16 melanoma cells, and found that α- Arbutin had a similar effect to β- Arbutin, but when the concentration of 1mmol/L, no α- Arbutin inhibited the growth of melanin cells, while β- Arbutin suppressed the same concentration, destroying the proliferation function of melanocyte cells, suggesting that cytotoxicity should not be ignored.
If the metabolism of melanin cells is destroyed or suppressed, it will produce some diseases, such as the genetic disease albinism, associated with a malignant tumor called melanocystoma (melanoma). This shows that α-arbutin has higher safety than β- Arbutin.
As the production technology keeps improving, the pricing for arbutin goes down a lot compared with the pricing years ago, you are welcome to contact us for any inquiry.