Advancements in molecular biology has greatly reshaped the pharmaceutical and biotechnology industry over the last couple of decades. Rapid innovations in healthcare technology has also boosted growth of pharmaceuticals verticals, including alkaline proteases market scenario.
Enzymes have long been used as alternatives to chemicals to improve the efficiency and cost-effectiveness of a wide range of industrial systems and processes. Alkaline proteases also known as basic proteases are a group of enzymes used primarily as additives in detergents and are active in a neutral to alkaline pH range. Most alkaline proteases have an optimal pH of around 10, with an isoelectric point of around pH 9. These are produced by alkalophilic micro-organisms and can resist extreme alkaline environments produced by a wide range of alkalophilic microorganisms. Alkaline proteases are obtained from various microbial sources such as fungi, bacteria, and certain yeasts.
Alkaline Proteases Market Dynamics
Alkaline protease enzymes demonstrate high stability and resistance to proteolytic hydrolysis, owing to their high degree of cross-linking to hydrogen bonds, disulphide bonds, and hydrophobic interactions. They are stable in association with chelating agents and perbonates. Developments in field of protein engineering coupled with development of industrial enzymes is expected to create substantial demand for industry players in artificial proteases market.
Alkaline Proteases Market Taxonomy
The global alkaline protease market outlook can be segmented on the basis of:
Serine protease and metalloprotease are the two types of alkaline proteases. They are also classified as endo-peptidases and exo-peptidases based on the position of the peptide bond cleavage.
Alkaline Proteases Market Applications
On the basis of application, the alkaline proteases market size has been classified into detergents, pharmaceuticals, meat tenderizers, protein hydrolyzates, food products, and waste processing. Alkaline proteases play a crucial role in the bioprocessing of used X-ray or photographic films for silver recovery. The use of alkaline proteases in detergents is being increasingly preferred over conventional synthetic ones due to their better cleaning properties, safer dirt removal conditions, and higher performance efficiency at lower washing temperature. Immobilized alkaline protease obtained from Bacillus subtilis has been studied for development of ointment compositions, non-woven tissues, gauze, and new bandage materials. Aspergillus oryzae derived proteases are used as a diagnostic aid in certain lytic enzyme deficiency syndrome. Alkaline proteases with keratinolytic activity are being explored in feather degradation and feather meal production for glues, fertilizers, biodegradable foils, and films.
Bacillus Species: Major Source of Alkaline Proteases
Alkaline protease enzymes can be obtained from bacterial and fungal sources. Bacillus Species is often commercially used in bioremediation mixes, or as probiotic agent in aquaculture. Other sources include Aspergillus species, Issatchenkia orientalis, Yarrowia lipolytica, Aureobasidium pullulans, and Cryptococcus aureus. Bacillus licheniformis and Bacillus coagulans can be used profitably for large scale production of alkaline protease. Alkaline protease from B. subtilis was used for management of waste feathers from poultry slaughterhouse.
Also, alkaline proteases obtained from fungal origin offers an advantage of separation due to easy removal of the mycelia from the final product by simple filtration. Moreover, the fungus can be grown in inexpensive substrates.
Increasing number of Studies being conducted to Increase Stability and Explore Additional Applications in Alkaline Proteases Market
High production cost is inhibiting the widespread use of extracellular enzymes for remediation. Technological development in the field of immobilized enzymes offers possibility of wider and economical use of these enzymes. Advancements in microbiology and biotechnology have created a favorable condition for development of proteases. Extensive studies are underway to increase stability to pH, temperature, organic solvents, reuse, and recovery of enzymes with the help of various enzyme immobilization techniques such as whole cell and cell free immobilization techniques. Characterization of enzymes, isolation and identification of promising strains, and optimization of products is a continuous process for improving existing application and also discovering potential application areas.
North America and Europe to dominate the alkaline proteases market size throughout the forecast period
Presence of wide range of end-user industries ranging from pharmaceutical industries to food & beverages processing companies along with high spending on industrial infrastructure is expected to boost the alkaline proteases market revenue growth in North America. Geographically, North America and Europe are expected to capture a major chunk of the market between 2016 and 2024. The market in Asia Pacific, primarily driven by China and India, is expected to burgeon at a significant rate over the forecast period.
Ab Enzymes, Acumedia Manufacturers, Inc., Advanced Enzymes, Novozymes, Noor Enzymes, Royal DSM, Sigma Aldrich Corporation, Solvay Enzymes and Specialty Enzymes & Biotechnologies Co. are some of the key players in the global alkaline proteases market.
Alkaline Proteases Market Key Developments
Key players in the market are focused on expanding their product portfolio. For instance, in July 2018, Royal DSM introduced PreventASe XR, an enzymatic solution that prevents the formation of acrylamide in high-pH applications to extend use of enzymatic acrylamide-reduction solution to more snacks and baked goods.
Major market players are also focused on expanding their geographical presence to enhance their market share. For instance, in June 2019, Novozymes started a new office in Kenya with the objective to expand its presence in East Africa. Moreover, the company was named the most innovative company in Denmark by European Patents Office in March 2019.