Related Experiment Video
Updated: Jun 3, 2026
08:10
Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System
Published on: August 8, 2016
Feed enzyme technology: present status and future developments.
Velmurugu Ravindran1, Jang-Ho Son
1Institute of Food, Nutrition and Human Health, Massey University, Palmerston North 4442, New Zealand. V.Ravindran@massey.ac.nz
Recent Patents on Food, Nutrition & Agriculture
|March 25, 2011
Summary
Exogenous enzymes improve animal feed digestibility and performance in poultry and pigs. Future trends and innovations in feed enzyme technology will drive increased adoption across animal agriculture.
Area of Science:
- Animal Science
- Biotechnology
- Nutritional Science
Background:
- Exogenous enzymes are established feed additives for poultry and pigs.
- They enhance nutrient digestion and animal performance by mitigating anti-nutritional factors.
Purpose of the Study:
- To provide an overview of current feed enzyme technology, including types and mechanisms.
- To discuss factors causing variable responses to enzyme supplementation.
- To highlight future trends and innovations in feed enzyme development and application.
Main Methods:
- Literature review of feed enzyme technology.
- Analysis of factors influencing enzyme efficacy.
- Discussion of emerging markets and patent landscape.
Main Results:
- Feed enzymes are crucial for improving feed efficiency and animal health.
- Variability in animal response is a key challenge, influenced by factors like diet composition and enzyme characteristics.
- Next-generation enzymes and evolving animal production practices will increase enzyme use.
Conclusions:
- The use of exogenous enzymes in animal feed is projected to grow significantly.
- Emerging markets include aquaculture and ruminant nutrition.
- Innovations in feed enzyme technology are critical for sustainable animal production.
Related Concept Videos
01:00Enzyme-linked Receptors
Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
01:27Upstream Processing
Upstream processing represents a critical phase in biomanufacturing, wherein biological systems such as microorganisms, mammalian cells, or insect cells are cultivated to produce therapeutic proteins, vaccines, enzymes, or other biologically derived products. This phase encompasses all steps from the selection and genetic manipulation of the production organism to the cultivation of cells in bioreactors under tightly controlled environmental conditions.Host Selection and Genetic OptimizationThe...
01:30Production of Pharmaceuticals
Industrial insulin production uses genetically engineered E. coli expressing a proinsulin gene controlled by a tryptophan promoter and containing a methionine linker for later cleavage. The cells also carry ampicillin resistance for selective growth. Seed cultures are stored at −80 °C and production begins by thawing a small amount to inoculate starter cultures, which are progressively scaled to a 50,000-L bioreactor. In the bioreactor, E. coli grow in nutrient-rich media under sterile, tightly...
01:22Bioreactor Controls-III
Strain improvement is a foundational strategy in industrial microbiology aimed at maximizing microbial productivity, particularly because natural isolates typically yield commercially valuable products in very low concentrations. Although optimizing the culture medium and environmental conditions can improve yields, these adjustments are inherently limited by the organism’s genetic potential. As a result, the focus shifts toward genetic modifications to enhance biosynthetic capacity. The...
01:07Catalytically Perfect Enzymes
The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
01:22Introduction to Enzymes
The use of enzymes by humans dates to 7000 BCE. Humans first used enzymes to ferment sugars and produce alcohol without knowing that this was an enzyme-catalyzed reaction. Wilhelm Kuhne coined the term 'enzyme' in 1877 from the Greek words ‘en’ meaning ‘in’ or ‘within’ and ‘zyme’ meaning ‘yeast.’
Most enzymes are proteins that speed up biochemical reactions without being consumed. Enzymes contain one or more active sites that bind the substrates and convert them into products. Many enzymes also...
Most enzymes are proteins that speed up biochemical reactions without being consumed. Enzymes contain one or more active sites that bind the substrates and convert them into products. Many enzymes also...