PRODUCT ADVANTAGES
High Immunoglobulin Content and Biological Activity
Kangping Bio’s bovine colostrum products demonstrate superior performance in both the quantitative content and functional bioactivity retention of immunologically active components. The product portfolio spans standard grades with 15%–30% IgG content, mid-to-premium grades with 30%–40% IgG content, and premium customized grades with 40%–50% IgG content. A higher baseline IgG concentration enhances the initial payload of immunoactive components per unit mass, thereby establishing a robust material basis for bovine colostrum’s physiological role in supporting immune homeostasis. Bovine colostrum IgG is a naturally occurring bioactive protein; following oral ingestion, a portion undergoes degradation and activity loss due to exposure to gastric acid and digestive enzymes. Consequently, formulations with elevated initial IgG content yield a greater absolute quantity of intact, biologically active IgG reaching the intestine—thereby partially compensating for digestive attrition, improving the likelihood of engagement at intestinal effector sites, thereby establishing the fundamental conditions for its localized immunomodulatory efficacy.
To maximize preservation of the biological activity of functional components, Kangping Bio has implemented a fully integrated low-temperature manufacturing platform—incorporating advanced unit operations including low-temperature fat separation, ceramic membrane cold sterilization, ultrafiltration-based concentration, and vacuum freeze-drying, while eliminating high-temperature treatment throughout. This strategy effectively prevents thermal denaturation and inactivation of thermolabile bioactive molecules such as immunoglobulins, thereby preserving their native structural integrity and biological activity to the greatest extent possible. As a result, the finished product demonstrates consistent and robust efficacy, fulfilling the stringent requirements of high-end markets for premium-quality ingredients.
References
[1] BORAD S G, SINGH A K, KAPILA S, BEHARE P, ARORA S, SABIKHI L. Influence of unit operations on immunoglobulins and thermal stability of colostrum fractions[J]. International Dairy Journal, 2019, 93: 85-91.
[2] CIVRA A, FERRARO S, CACCIA E, et al. Antirotaviral activity of dairy byproducts enriched in fractions from hyperimmune bovine colostrum: the effect of thermal and high hydrostatic pressure treatments[J]. Food & Function, 2024, 15(5): 2265-2281.
[3] MANN S, LEAL W V, SANTOS G T, et al. Heat treatment of bovine colostrum: I. Effects on bacterial and somatic cell counts, immunoglobulin, insulin, and IGF-I concentrations, as well as the colostrum proteome[J]. Journal of Dairy Science, 2020, 103(3): 2840-2852.
[4] DAS A, SETH R, TARAFDAR A, DEY S, KUMAR Y, SIROHI R. Changes in techno-functional characteristics of cow colostrum powder prepared by freeze drying[J]. Journal of Food Quality, 2024, 2024: 2608059.
[5] Tacket CO, Losonsky G, Link H, Hoang Y, Guesry P, Hilpert H, et al. Protection by milk immunoglobulin concentrate against oral challenge with enterotoxigenic Escherichia coli. N Engl J Med. 1988;318(19):1240-1243.
[6] Kelly CP, Chetham S, Keates S, Bostwick EF, Roush AM, Castagliuolo I, et al. Survival of anti-Clostridium difficile bovine immunoglobulin concentrate in the human gastrointestinal tract. Antimicrob Agents Chemother. 1997;41(2):236-240.
[7] Sarker SA, Casswall TH, Mahalanabis D, Alam NH, Albert MJ, Brüssow H, et al. Successful treatment of rotavirus diarrhea in children with immunoglobulin from immunized bovine colostrum. Pediatr Infect Dis J. 1998;17(12):1149-1154.
[8] Warny M, Fatimi A, Bostwick EF, Laine DC, Lebel F, LaMont JT, et al. Bovine immunoglobulin concentrate-Clostridium difficile retains C difficile toxin neutralising activity after passage through the human stomach and small intestine. Gut. 1999;44(2):212-217.
Hydrolyzed Bovine Colostrum Peptides
Kangping Bio’s proprietary enzymatic hydrolysis technology for bovine colostrum proteins has been granted a national invention patent (Patent No. ZL201310279512.1). Employing a precisely controlled, multi-enzyme hydrolysis process, the patented technology selectively cleaves high-molecular-weight milk proteins above 100,000 Daltons—including hard-to-digest casein fractions—into low-molecular-weight peptide fragments below 2,000 Daltons. The process applies moderate, controlled hydrolysis (optimal degree of hydrolysis: 44%–45%), ensuring degradation of indigestible macromolecular proteins while preserving the structural integrity and bioactivity of key immunomodulatory components native to bovine colostrum to the greatest extent possible. While retaining the core nutritional components of native bovine colostrum, the resulting hydrolysate offers advantages including improved solubility, reduced allergenicity, and improved nutrient bioavailability, thereby enabling broad applicability in high-end dairy formulations, including partially hydrolyzed formulas and hypoallergenic formulations.
No. | Product Feature | Detailed Description |
|---|---|---|
1 | Improved Solubility | Natural bovine colostrum is rich in high-molecular-weight proteins, which exhibit limited aqueous solubility and poor dispersibility, and are highly sensitive to variations in temperature and pH. These physicochemical limitations substantially hinder its compatibility and processability in finished-product formulation. Through a proprietary, controlled enzymatic hydrolysis process, these poorly soluble, high-molecular-weight proteins are selectively cleaved into low-molecular-weight peptide fractions with markedly enhanced aqueous solubility and physicochemical stability. This product demonstrates rapid and homogeneous dissolution across the conventional processing and reconstitution temperature range (20–60 °C) and exhibits expanded tolerance to temperature and pH variations—significantly improving process compatibility and formulation versatility. |
2 | Reduced Allergenicity | In milk-based products, macromolecular proteins such as β-lactoglobulin constitute the primary sources of allergenicity, and the specific antigenic epitopes on their surfaces are the core drivers of gastrointestinal intolerance and mild allergic responses. Leveraging a precisely controlled multi-enzyme hydrolysis process, the patented technology selectively targets and degrades allergenic macromolecular milk proteins, effectively disrupting the spatial conformation of allergenic epitopes—eliminating allergen sources at the origin and substantially reducing the product’s potential allergenic risk. |
3 | Improved Nutrient Bioavailability | Intact native milk proteins exist as macromolecular complexes that must undergo sequential hydrolysis by multiple gastrointestinal proteases prior to absorption and metabolic utilization. In contrast, low-molecular-weight bioactive peptides are absorbed rapidly and efficiently via the intestinal epithelium’s dedicated peptide transporter, circumventing extensive proteolytic digestion and thereby enabling faster uptake and improved bioavailability. This product employs a patented in-vitro enzymatic hydrolysis process to break down macromolecular proteins under controlled conditions, yielding a nutrient profile enriched in bioavailable small-molecule peptides. As a result, gastrointestinal digestive load is reduced, and overall nutrient absorption and utilization efficiency are enhanced. |
References
[1] Riaz, S., Imran, A., Rasheed, M., Amjad, A., Shankar, A., Chauhan, G., Basharat, Z., Islam, F., Naeem, U., & Ndagire, C. T. (2026). Health benefits and value addition of bovine colostrum (BC): a comprehensive review of its nutritional and functional potential. Food Science of Animal Resources, 46, 55.
[2] Liang, X., Yang, H., Sun, J., Cheng, J., Luo, X., Wang, Z., Yang, M., Tao, D. B., Yue, X., & Zheng, Y. (2021). Effects of enzymatic treatments on the hydrolysis and antigenicity reduction of natural cow milk. Food Science & Nutrition, 9(2), 985–993.
[3] Halavach, T. M., Kurchenko, V. P., Tarun, E. I., Dudchik, N. V., Yatskou, M. M., Lodygin, A. D., Alieva, L. R., Evdokimov, I. A., & Ulrih, N. P. (2023). Influence of complexation with β- and γ-cyclodextrin on bioactivity of whey and colostrum peptides. International Journal of Molecular Sciences, 24(18), 13987.
[4] Fajardo-Espinoza, F. S., Ordaz-Pichardo, C., Sankar, U., Romero-Rojas, A., Moreno-Eutimio, M. A., & Hernández-Sánchez, H. (2021). In vitro cytomodulatory and immunomodulatory effects of bovine colostrum whey protein hydrolysates. International Journal of Food Science and Technology, 56(5), 2109–2121.
[5] Liang, X., Wang, Z., Yang, H., Luo, X., Sun, J., Yang, M., Shi, X., Yue, X., & Zheng, Y. (2022). Evaluation of allergenicity of cow milk treated with enzymatic hydrolysis through a mouse model of allergy. Journal of Dairy Science, 105(2), 1039–1050.
[6] Playford, R. J., Weiser, M. J., & Marchbank, T. (2021). Methods to improve efficacy of orally administered bioactive peptides using bovine colostrum as an exemplar. PLOS ONE, 16(6), e0253422.
[7] Chiang, S. H., Wang, S. Y., Chang, C. Y., & Chen, C. W. (2017). Bovine colostrum whey protein hydrolysate inhibits cell DNA damage and LDL oxidation in vitro. Molecules, 22(3), 456.
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