Huijia Group was established in 2007, driven by synthetic biotechnology, focusing on the core needs of users, with high quality, low price, and convenience, to build a product system and operation system. Based on a profound understanding and research of the physiological process of living organisms, Huijia integrates the concept of green technology into new biotechnology and innovative formulation processes. Care more, as a subsidiary of Huijia Group, helps to enhance products through fermentation processes. As a national high-tech enterprise, Vegamax has established 6 production bases and has many years of experience in the production of food ingredients and animal health products. As a leader in the microbial fermentation industry, we have 20 years of fermentation experience and effectively improve bioavailability.
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Our Factory
Huijia Group was established in 2007, driven by synthetic biotechnology, focusing on the core needs of users, with high quality, low price, and convenience, to build a product system and operation system.
Our Product
Care More has a rich product catagory, and its products and services provide veterinarians, farmers and pet owners, food & cosmetic industry with a comprehensive series of products and knowledge services to help them deal with the various problems that may arise during the process, making health problems easier to deal with. The products mainly include animal, pet, food, cosmetics, plant.
Professional R&D Team
The Green Technology Research Institute is headed by Dr. Yang Caimei, a professor/doctoral supervisor at Zhejiang Agriculture and Forestry University and a provincial expert in Zhejiang Province. Currently, the research and development team has more than 50 master's and doctoral level R&D talents from Zhejiang University, Tsinghua University, and Max Planck Institute in Germany, including 8 PhDs, 32 graduate students, 5 national level experts, and 2 international consultants.
Our Service
Care more, standing on shoulder of giants, invest 20 years' innovation in microbiology and specialty ingredient to provide green solutions for livestock and companion animals, human and plant, through passionated & experienced team in industry, finally deliver supreme value to customer.
LysoPro is a fermented modified lysozyme with significantly improved antibacterial and antiviral capabilities than egg white lysozyme and enter the bloodstream.
SmartPond is a combination of 4 probiotics for bio-remediation. Probiotic especially anaerobic bacteria can not only relieve black and smelly bottom but also regulate water quality without oxygen consumption in pond.
P-Care is a postbiotic (swine poultry antibacterial peptide) derived from the fermentation of probiotics, serving as an antibiotic-free solution against Gram-negative bacteria such as Salmonella and E.coli. Currently, extensive researches have been conducted on the active metabolites of probiotics, including exopolysaccharides, bacteriocins, organic acids, short-chain fatty acids, and vitamins. These dynamic metabolites have demonstrated remarkable properties in terms of their anti-inflammatory, anti-tumor, antioxidant effects while also exhibiting immune-modulating capabilities and potential for prevention or treatment of various metabolic diseases.
VibPro is aqua antibacterial peptide derived from probiotic fermentation, offering an antibiotic-free solution to combat diseases caused by vibrio such as AHPND/EMS/TPD etc.. With the rapid expansion and increasing scale of the marine aquaculture industry, there has been a surge in bacterial diseases in this sector. Vibrio species including V. anguillarum, V. harveyi, V. parahaemolyticus, and V. alginolyticus pose a significant threat to animal health and result in substantial economic losses.
P-Care is a postbiotic derived from the fermentation of probiotics, serving as an antibiotic-free solution against Gram-negative bacteria such as Salmonella and E.coli. Currently, extensive researches have been conducted on the active metabolites of probiotics, including exopolysaccharides, bacteriocins, organic acids, short-chain fatty acids, and vitamins. These dynamic metabolites have demonstrated remarkable properties in terms of their anti-inflammatory, anti-tumor, antioxidant effects while also exhibiting immune-modulating capabilities and potential for prevention or treatment of various metabolic diseases.
GutUp is a combination of bacillus coagulans and clostridium butyricum which are stable and acid-producing bacteria
Antimicrobial peptides are short-chain amino acid sequences produced by all living organisms in self-defense. Antimicrobial peptides have a broad spectrum of antibacterial, antifungal, antiparasitic, and antiviral properties. Recent research has focused on introducing antimicrobial peptides into polymer matrices with applications in medicine, food packaging, personal care, and pharmacy. Antimicrobial peptides in AP materials appear to be a promising strategy for minimizing food deterioration, improving food security, and maintaining quality.
Advantages of Liquid Antimicrobial Peptide
It can participate in repairing the intestine barrier to prevent the bacteria entering blood and reducing the translocation, regulating the synthesis of intestinal epithelial tight connections, thus promoting intestinal maturation and repairing stress damage. More and more studies have shown that probiotic metabolites play a role in the early intestinal development of animals, immune system differentiation, epithelial cell proliferation and other intestinal growth and development processes
The efficacy of this treatment extends to both G- and G+ bacteria, particularly targeting salmonella and E.coli, as it disrupts the integrity of their cell membranes. By inducing the formation of transmembrane ion channels, the membrane is compromised, leading to cellular leakage and ultimately resulting in cell death.
Probiotic metabolites exert antibacterial effects through different mechanisms of action, including disrupting the integrity of cell membranes, interfering with nucleic acid functions, affecting protein synthesis, and regulating related enzyme activity. This characteristic makes it unlikely to cause drug resistance and side effects, and allows for long-term therapeutic and preventive applications during the farming.
Probiotics can produce a variety of active metabolites, such as short-chain fatty acids, hydrogen peroxide, conjugated linoleic acid, low-fructose oligosaccharides, and bacteriocins, to exert their probiotic effects. These products have been verified by third-party tests and do not contain antibiotic components, making them green and safe. Especially in areas where antibiotics are banned, they can effectively replace antibiotics to exert antibacterial effects.
Antimicrobial peptides are a unique and diverse group of molecules, which are divided into subgroups on the basis of their amino acid composition and structure. Antimicrobial peptides are generally between 12 and 50 amino acids.
These peptides include two or more positively charged residues provided by arginine, lysine or, in acidic environments, histidine, and a large proportion (generally >50%) of hydrophobic residues.The secondary structures of these molecules follow 4 themes, including i) α-helical, ii) β-stranded due to the presence of 2 or more disulfide bonds, iii) β-hairpin or loop due to the presence of a single disulfide bond and/or cyclization of the peptide chain, and iv) extended.
Many of these peptides are unstructured in free solution, and fold into their final configuration upon partitioning into biological membranes. The peptides contain hydrophilic amino acid residues aligned along one side and hydrophobic amino acid residues aligned along the opposite side of a helical molecule.This amphipathicity of the antimicrobial peptides allows them to partition into the membrane lipid bilayer. The ability to associate with membranes is a definitive feature of antimicrobial peptides, although membrane permeabilization is not necessary. These peptides have a variety of antimicrobial activities ranging from membrane permeabilization to action on a range of cytoplasmic targets.
Supplement conventional antibiotics and there are now a number of products available on the veterinary market that utilise anti-microbial peptides (AMP's), either through the addition of synthetic AMP's or through the inclusion of compounds known to stimulate production of naturally occurring ones.
AMP's are small, cationic polypeptides which play a fundamental role in the innate immune system. They possess broad spectrum activity against bacteria, viruses and fungi, and modify the local inflammatory response through promotion of leucocyte chemotaxis. They are secreted from epithelial and immune cells, with upregulation occurring in the face of infection or injury. The two major sub-families in mammals are defensins and cathelicidins, which exhibit similar physical and functional properties.
In the face of invasion from a pathogen, AMP's are involved in many different processes such as the recruitment of other immune cells and through more direct effects on bacteria/fungi. Defensins can directly attach to the cell wall of these pathogens and due to being positively charged, they are drawn into the negatively charged cell membrane and pair up to create a pore, ultimately causing cellular disruption and death.
The potential importance of skin defensins has been highlighted in studies of various skin disorders, for example the comparison of lesional skin from humans with atopic dermatitis (AD) to the skin of humans with psoriasis. The former group demonstrate a significantly lower defensin expression and are more prone to skin infection, despite both conditions being associated with a defective skin barrier. It has therefore been hypothesised that a decreased production of AMP's or production of non-functional AMP's could be a possible cause of the higher susceptibility to skin infection in AD. However, in contrast to this, other studies have noted a significant increase in the expression of some AMP's in both human and canine AD patients.
Harnessing this knowledge for therapeutic application is an area of increasing interest; certain plant extracts affect levels of AMP's and a recent study in atopic dogs demonstrated a reduction in Staphylococcus spp. after 14 days of daily treatment with a water based spray containing 0.1% Peumus boldus leaf and Spiraea ulmaria, compared to a control group who just received a water based spray4.
From conducted studies, it's clear that AMP's are an important component of the innate immune system to defend against external micro-organisms and clearly warrant further investigation with regards to their role in modulating skin disease and how they can be utilised further as therapeutic agents.
Mechanisms of Action of Liquid Antimicrobial Peptide
Antimicrobial peptides generally have a net positive charge, allowing them to interact with the negatively charged molecules exposed on bacteria and cancer cell surfaces, such as phospholipid phosphatidylserine, O-glycosylated mucins, sialylated gangliosides, and heparin sulfates. The mechanism of action of these peptides varies widely but can be simplified into two categories: membranolytic and non-membranolytic antimicrobial peptides.The disruption of membranes by membranolytic antimicrobial peptides can be described by four models:
Barrel-stave model: The barrel-stave model proposes that AMPs interact with the lipid bilayer of the microbial cell membrane to form transmembrane channels or "barrel staves". These channels are thought to disrupt the membrane's integrity, leading to the death of the microbe.
Carpet model: The carpet model proposes that AMPs adsorb onto the lipid bilayer of the microbial cell membrane, forming a dense layer that causes the membrane to become permeabilized. This model suggests that the AMP acts as a "carpet" that covers the surface of the cell, preventing the microbe from functioning properly.
Toroidal model: The toroidal model proposes that AMPs interact with the lipid bilayer of the microbial cell membrane to form toroidal structures, which are thought to pinch off sections of the membrane and lead to the formation of vesicles. This process is thought to disrupt the membrane's integrity and cause the death of the microbe.
Disordered toroidal-pore model: According to this model, the disordered AMPs wrap around the lipid bilayer and create a pore, which disrupts the membrane's integrity and leads to the death of the microbe. Unlike the toroidal model, which suggests that the AMP creates a stable toroidal structure, the disordered toroidal-pore model suggests that the AMP is flexible and does not form a stable toroidal structure. The peptide-lipid pore complex becomes intrinsically disordered, with the orientation of the peptide not well defined.
Several methods have been used to determine the mechanisms of antimicrobial peptide activity. In particular, solid-state NMR studies have provided an atomic-level resolution explanation of membrane disruption by antimicrobial peptides. In more recent years, X-ray crystallography has been used to delineate in atomic detail how the family of plant defensins rupture membranes by identifying key phospholipids in the cell membranes of the pathogen. Human defensins have been thought to act through a similar mechanism, targeting cell membrane lipids as part of their function.
The cationic antimicrobial peptides are an important component of the innate defenses of all species of life. Such peptides can be constitutively expressed or induced by bacteria or their products. The best peptides have good activities vs. a broad range of bacterial strains, including antibiotic-resistant isolates. They kill very rapidly, do not easily select resistant mutants, are synergistic with conventional antibiotics, other peptides, and lysozyme, and are able to kill bacteria in animal models. It is known that bacterial infections, especially when treated with antibiotics, can lead to the release of bacterial products such as lipopolysaccharide (LPS) and lipoteichoic acid, resulting in potentially lethal sepsis.
In contrast to antibiotics, the peptides actually prevent cytokine induction by bacterial products in tissue culture and human blood, and they block the onset of sepsis in mouse models of endotoxemia. Consistent with this, transcriptional gene array experiments using a macrophage cell line demonstrated that a model peptide, CEMA, blocks the expression of many genes whose transcription was induced by LPS. The peptides do this in part by blocking LPS interaction with the serum protein LBP. In addition, CEMA itself has a direct effect on macrophage gene expression. Because cationic antimicrobial peptides are induced by LPS and are able to dampen the septic response of animal cells to LPS, we propose that, in addition to their role in direct and lysozyme-assisted killing of microbes, they have a role in feedback regulation of cytokine responses. We are currently developing variant peptides as therapeutics against antibiotic-resistant infections.
Antibiotics are widely used for disease prevention and growth promotion in conventional livestock and poultry production. Concurrent with the success of antibiotics for treating infections, the emergence and rapid dissemination of antibiotic-resistant bacteria poses substantial risks for animal and human health. Now, antibiotic resistance has become an increasingly serious problem. The global human deaths are predicted to reach 10 million by 2050 due to antibiotic resistant infections, which are more than the current death toll associated with different forms of cancer. For this reason, there is an urgent need to develop novel antimicrobial agents, such as alterative drugs based on antimicrobial peptides (AMPs).
AMPs are produced by a variety of organisms and are responsible for protecting the host against the pathogens, as a component of innate immunity. AMPs are generally between 12 and 50 amino acids with a broad spectrum of antibiotic activities against bacteria, yeasts, fungi, and viruses, as well as cytotoxic activity on cancer cells, anti-inflammatory, and immunomodulatory activities. For now, based on their secondary structure, AMPs fit into four major classes. Cell membrane permeabilization by AMPs was thought to be the primary mechanism of killing pathogenic microbes or cancer cells.
In recent years, studies on AMPs and their applications have become one of the hot spots in different fields, especially in agricultural science. AMPs are considered as one of the most promising alternatives to conventional antibiotics, and have a strong potential for application as feed additives in swine, poultry and even fish production. Some studies show AMPs as feed additives have remarkable effects compared with the traditional antibiotics, including:
Broad-spectrum (antibacterial, antifungal, and antiviral) effects
Low levels of induced resistance
Improve growth performance
Promote nutrient digestibility
Modulation of gut microbiota
Enhance immune function
In addition, AMPs not only represent alternatives to antibiotics as antimicrobial growth promoters (AGP) but are also as excellent therapeutic agents for animal disease prevention, control, and treatments through directly adding to animal feed as anti-infective additives to protect animals.
Being a team with excellent experience in feed science and animal nutrition, Lifeasible provides a series of AMPs' services against feed additives to satisfy agricultural developer requirements for green health and safety animal feed additives, including:
AMPs synthesis service
AMPs activity assay service
AMPs development
AMPs modification and design
Nuclear magnetic resonance (NMR) has played a significant role in determining the structural details of AMPs. An analysis of the peptide's three-dimensional structure has offered a deeper insight into their functions. Two-dimensional NMR methods are mainly used for obtaining three-dimensional structures for small-sized AMPs that can be divided into five classes according to their secondary structure. Although these peptides remain unstructured in the solution, they may adopt specific structural characteristics after coming in contact with the membrane. Four such structural characteristics have been observed, namely alpha-helical, beta stranded, beta-hairpin or loop, and extended conformation. The structure is either confirmed by NMR, CD, or homology modeling studies, where the atomic structure of the target sequence is constructed from its amino acids and the three-dimensional structure of a template. Most of the AMPs belong to the α-helical conformations. A large number of sequences have been reported in this class, which includes both naturally isolated and chemically synthesized peptides. In an aqueous solution, α-helical AMPs have a linear structure, and upon contact with a bacterial membrane or organic solvent, it forms an amphipathic helical structure. The amphipathic helical structure allows the α-helix AMPs to burrow deep into the phospholipid bilayer and disrupt the membrane integrity. The Myeloid antimicrobial peptide from different farm animals, namely BMAP-27, SMAP-29, and PMAP-23, all possess anα-helix as their secondary structure.
In general, β-sheet AMPs are cyclic molecules composed of at least two antiparallel β-sheets stabilized by intramolecular disulfide bonds. The β-sheet peptides are more ordered in an aqueous solution due to their rigid structure and do not undergo a drastic conformation shift like helical peptides upon membrane interaction. Unlike α-helix, the mechanistic model behind the β-sheet antimicrobial activity is not well understood. The β-sheet peptides contain primarily plant defensins, mammal α defensins and β defensins (BNBDs, Bovine β defensin-1, porcine β-defensin), insect defensins, proline-rich antibacterial peptides, protegrin, and tachyplins. Defensins are the well-researched β-sheet peptides that are formed in neutrophils, macrophages, and epithelial cells as inactive precursors. Protegrin groups of AMPs from porcine have a well-elucidated structure. Members of the protegrin group, PG-1 PG-2 PG-3, and PG-5are composed of two antiparallel β-sheets connected by a β turn.
Loop AMPs have a loop structure stabilized by amide, disulfide, and isopeptides bonds. Thanatin, a prominent member of this group is isolated from the spinning soldier bug. A single disulfide bond between residue 11 and 18 stabilizes and offers thanatin its characteristic structure.
Extended peptides lack the classical secondary structure. Oftentimes, they are rich in certain amino acids, including residues of glycine, arginine, tryptophan, proline, and histidine. The structure is stabilized by hydrogen bond and Vander Waal interactions with the phospholipid bilayer. Indolicidin has an extended poly-L-proline II helix as a secondary structure; however, in a neutral DPC environment, the peptide backbone takes a boat shape. Several AMPs do not belong to any of these classes, and some appear only in aggregated form or when communicating with the membrane. The plant-derived circulin A is a clear example of this, consisting of a combined α-helix and β-sheet structure that forms the cyclic cysteine knot.
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