The Effect of Fermentation Conditions and Stress Factors on Production of Transglutaminase by Streptomyces spp.

Abstract

The use of transglutaminase (TG) enzyme in food processing has led to considerable changes in the functional properties of proteins through cross-linking reactions. The TG enzyme catalyses the acyl transfer reactions leading to the formation of covalent cross-links between various primary amines, peptides, and proteins, thereby causing these changes. Animal and microbial sources (Streptomyces sp.) can be used for commercial production of transglutaminase. Microbial-derived TG enzyme takes priority in food and other industries because of the need for calcium ions of animal-derived TG enzyme and the cost of production. Efforts to increase microbial transglutaminase (mTG) enzyme production are continuously developing and are a highly dynamic research area. In recent years, attempts have been made to re-optimize production processes using different fermentation strategies and recombinant DNA techniques. For mTG enzyme production, intensive and different studies are being carried out on some classical strategies such as substrate optimization, metabolic optimization and control of fermentation conditions (pH, dissolved oxygen, temperature, mixing and aeration rate, etc.). On the other hand, the impact of microbial stress factors (rapid change of temperature and pH, presence of certain salts and alcohols, etc.) as a new strategy to increase mTG production has also begun to be investigated and studied in a limited number of studies. In this review, several strategies for increasing the biosynthesis of the enzyme have been emphasized in order to make the production of mTG enzymes more efficient and cost-effective by increasing the use in many fields.