Ferment-derived HA complex aids skin health

James V Gruber, Ezgi Todurge – BotanicalsPlus, US

Hyaluronic acid (HA) has been one of the most popular polysaccharides to appear in personal care products in the last decade.1,2


molecule was originally isolated from Rooster combs where it was available in significant amounts and at high molecular weight.3 However, it has now been found that several microorganisms can produce appreciable quantities of the glucosaminoglycan also at high molecular weights.4

In addition, with the

discovery of Hyaluronidase (a key enzyme that breaks down high molecular weight HA), it is now possible to commercially create various molecular weight fractions of HA from very high (1.5-2 Million Daltons (MDa*)) to very low (5-20 Kilo Daltons (kDa)).5 Today, the topical benefits of HA are widely

known and recognised by scientists and consumers. HA is renowned for its water-binding capabilities and is often suggested to be able to bind many times its weight in water molecules— but this behaviour is keenly dependent on the HA’s molecular weight.6

The human body itself

manufactures HA and it has been suggested that the body may contain nearly 0.02% hyaluronic acid as a function of total body mass—but over a third of it is lost daily.7

humors of the eye, in the cartilage of the bones and most importantly, it is abundant in the dermis, epidermis and in small amounts in the stratum corneum. Along with the components of the skin’s Natural Moisturizing Factor (NMF), HA is a critical element for maintaining the skin’s natural hydration.8 Aside from its ability to bind water, HA

has an ability to also signal skin cells. This ability to transmit cellular messages appears to be molecular weight dependent— with lower molecular weight fragments able to penetrate to skin cells to create messages, while higher molecular weight portions signal cellular responses by contacting receptor proteins that are embedded in the skin cell membranes like small HA-focused antenna. One transmembrane protein that HA binds to is called Extracellular Matrix-III (ECM-III) (also known as the Hyaluronate Receptor protein) that is an important Cell Adhesion Molecule (CAM)9-10

(Figure 1). This important protein is

responsible for numerous physiological effects that are triggered when the HA molecule interacts and binds to specific sites on the Hyaluronate Receptor. These binding sites are also known to have some molecular weight dependence. It is important to keep in mind

Figure 1: Schematic diagram of Hyaluronate Receptor protein binding to hyaluronic acid within a keratinocyte skin cell. Binding of hyaluronic acid to the Hyaluronate Receptor protein creates a glycoprotein conjugate that drives numerous skin cell functions including barrier formation, tight junction protein formation, Calcium ion flux and keratinocyte cellular proliferation and differentiation.

that high molecular weight HA that might be applied topically would unlikely be able to penetrate the living epidermis. So, these high molecular weight HA polysaccharides must be created within the viable dermis and epidermis of the skin to be able to bind to the ECM-III proteins. On the other hand, lower molecular weight fragments of HA are known to be able to penetrate to the viable epidermis where they can interact with the keratinocytes in the skin via the ECM-III proteins.11-12 While it was known that HA of various

molecular weights can interact in different respects with the Hyaluronate Receptor protein to elicit different skin effects, it was unknown if HA might also have some impact on the actual stimulation of formation of the ECM-III protein in skin cells. It has now been shown that indeed, a unique HA complex created from various molecular weight fractions of HA called BP—Triluronic®


[BotanicalsPlus®, Fairfield, NJ] can stimulate the expression of this critical Cell Adhesion Molecule in Normal Human Epidermal

July 2021 PERSONAL CARE HA is found in the vitreous


Page 1  |  Page 2  |  Page 3  |  Page 4  |  Page 5  |  Page 6  |  Page 7  |  Page 8  |  Page 9  |  Page 10  |  Page 11  |  Page 12  |  Page 13  |  Page 14  |  Page 15  |  Page 16  |  Page 17  |  Page 18  |  Page 19  |  Page 20  |  Page 21  |  Page 22  |  Page 23  |  Page 24  |  Page 25  |  Page 26  |  Page 27  |  Page 28  |  Page 29  |  Page 30  |  Page 31  |  Page 32  |  Page 33  |  Page 34  |  Page 35  |  Page 36  |  Page 37  |  Page 38  |  Page 39  |  Page 40  |  Page 41  |  Page 42  |  Page 43  |  Page 44  |  Page 45  |  Page 46  |  Page 47  |  Page 48  |  Page 49  |  Page 50  |  Page 51  |  Page 52  |  Page 53  |  Page 54  |  Page 55  |  Page 56  |  Page 57  |  Page 58  |  Page 59  |  Page 60  |  Page 61  |  Page 62  |  Page 63  |  Page 64  |  Page 65  |  Page 66  |  Page 67  |  Page 68  |  Page 69  |  Page 70  |  Page 71  |  Page 72  |  Page 73  |  Page 74  |  Page 75  |  Page 76  |  Page 77  |  Page 78  |  Page 79  |  Page 80  |  Page 81  |  Page 82  |  Page 83  |  Page 84