Alkaline Proteases Market Segments and Key Trends 2017-2025

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 of the alkaline proteases have an optimal pH of around pH 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. These are obtained from various microbial sources such as fungi, bacteria and certain yeasts. The 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.

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They are stable in association with chelating agents and perbonates. Bacillus licheniformis and Bacillus coagulans can be used profitably for large scale production of alkaline protease. Additionally, alkaline proteases obtained from fungal origin offer 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.

The global alkaline protease market can be segmented based on by type, by source, by application and geography. Type of alkaline proteases includes serine protease and metalloprotease. They are also classified as endo-peptidases and exo-peptidases based on the position of the peptide bond cleavage. Application segment has been further classified as detergents, pharmaceuticals, leather industry, meat tenderizers, protein hydrolyzates, food products and waste processing. Characterization of enzymes, Isolation and identification of promising strains and optimization of products is currently a continuous process for improving existing as well as unveiling new applications. Advances in microbiology and biotechnology have created a favorable condition for the development of proteases.

Bacillus species is the major source of alkaline proteases and is often commercially used in bioremediation mixes, or as probiotic agent in aquaculture. Others sources include Aspergillus species, Issatchenkia orientalis, Yarrowia lipolytica, Aureobasidium pullulans, and Cryptococcus aureus. High production cost is currently known to inhibit the widespread use of extracellular enzymes for remediation. Technological development in the field of immobilized enzymes offer possibility of wider and economical use of these enzymes. 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.

Alkaline protease from B. subtilis was used for the management of waste feathers from poultry slaughterhouse. 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 preferred now-a-days over the 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. At present, alkaline proteases with keratinolytic activity are being explored in feather degradation and feather meal production for glues, fertilizers, biodegradable foils and films.

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 protease market.

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