There are many contributing factors leading to poor digestion – ageing, stress, genetics, excess alcohol consumption and malnutrition. Poor nutrition may result in low fibre intake and bowel flora imbalance. Inefficient enzyme production may also lead to detrimental health outcomes. As health practitioners, we know addressing dietary and lifestyle issues is a priority. Inclusion of raw foods (where appropriate) and enzyme supplementation where depletion is present may be warranted.
The gastrointestinal system produces and releases digestive enzymes to help catabolise fats, proteins, and carbohydrates, which in turn assists with healthy digestion and nutrient absorption. 
Digestive enzymes derived from microbial species may provide comprehensive support to aid digestive function. Microbe-derived enzymes are normally synthesised from fungal sources via a fermentation process. Some of these enzymes are also used in traditional food preparation. For example, Aspergillus oryzae is used in the fermentation process of soybeans to produce soy sauce, tamari and miso. 
Aspergillus oryzae is a filamentous (thread-like) fungi known to have prominent potential for the secretory production of several enzymes including amylase, protease and tilactase.  This strain shows high amylase activity for starch degradation.  Lipase is also synthesised from A.oryzae. 
Trichoderma longibrachiatum: A known cellulolytic fungi.[4,5] The cellulase activity of T. longibrachiatum may be linked with induction of xylanase activity. Parallels have been drawn between the relationship of hemicellulose and cellulose in plant biomass. 
Rhizopus oryzae: Research has highlighted that Rhizopus species family are important and versatile enzymes. 
In contrast to animal derived enzymes, microbial enzyme preparations may be more resistant to inactivation by stomach acid and possess broader activity throughout a wide range of pH conditions inherent to the digestive tract.  Microbial enzymes are also more active and stable than plant and animal enzymes and require a lower dosage to be effective. [8,9]
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2. Machida, M., Yamada, O., Gomi, K. (2008). Genomics of Aspergillus oryzae: Learning from the History of Koji Mold and Exploration of Its Future. DNA Research, (15), 173–183.
3. Kim, H., Kim, J., Bai, D., Ah, B-H. (2011). Identification and Characterization of Useful Fungi with α-Amylase Activity from the Korean Traditional Nuruk. Mycobiology, 39(4): 278–282.
4. Omojasola, P., Jilani, O. (2008). Cellulase Production by Trichoderma longi, Aspergillus niger and Saccharomyces cerevisae Cultured on Waste Materials from Orange. Pakistan Journal of Biological Sciences, 11: 2382-2388.
5. Royer, J. C., & Nakas, J. P. (1990). Interrelationship of Xylanase Induction and Cellulase Induction of Trichoderma longibrachiatum. Applied and Environmental Microbiology, 56(8), 2535–2539.
6. Serrano, A., Ferrer, P., Sola, C., Schmid, R., Valero, F. (2001). Optimization of the high-level production of Rhizopus oryzae lipase in Pichia pastori. Journal of Biotechnology, 86, 59–70.
7. Spiegel, K., Tasali, E., Penev, P., Van Cauter, E. (2004). Sleep curtailment in healthy young men is associated with decreased leptin levels, elevated ghrelin levels, and increased hunger and appetite. Annals of Internal Medicine, 141(11), 846-850.
8. Anbu, P., Gopinath, S., Cihan, A., Chaulagain, B. (2013). Microbial Enzymes and Their Applications in Industries and Medicine. BioMed Research International, (2013), doi:10.1155/2013/204014
9. Griffin, S. M., Alderson, D., & Farndon, J. R. (1989). Acid resistant lipase as replacement therapy in chronic pancreatic exocrine insufficiency: a study in dogs. Gut, 30(7), 1012–1015.
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