Feed & Additive Magazine Issue 51 April 2025

ISSUE FOCUS FEED & ADDITIVE MAGAZINE April 2025 49 “Trypsin inhibitors are naturally occurring proteins found predominantly in soybeans and other legumes. These inhibitors bind to trypsin—an essential enzyme responsible for breaking down dietary proteins into absorbable amino acids. When trypsin activity is compromised, protein utilization decreases, leading to reduced growth rates and impaired feed conversion efficiency.” In poultry nutrition, maintaining optimal feed efficiency is critical to achieving maximum growth and profitability. Because of the regional variability in feed quality, one significant challenge that nutritionists and feed mill managers frequently encounter is the impact of trypsin inhibitors in feed ingredients, particularly soybean meal. These inhibitors can significantly reduce protein digestion and impair performance, so it’s necessary to understand the science behind this anti-nutritional factor and how to effectively mitigate its impact. WHAT ARE TRYPSIN INHIBITORS? Trypsin inhibitors are naturally occurring proteins found predominantly in soybeans and other legumes. These inhibitors bind to trypsin—an essential enzyme responsible for breaking down dietary proteins into absorbable amino acids. When trypsin activity is compromised, protein utilization decreases, leading to reduced growth rates and impaired feed conversion efficiency. One of the key consequences of trypsin inhibitors is an increase in pancreatic enzyme secretion, which can result in pancreatic hypertrophy and reduced nutrient absorption.1 Additionally, the presence of trypsin inhibitors can cause intestinal irritation and inflammation, exacerbating nutrient loss and negatively affecting gut health.2 BREAKING THE CHAIN: COMBATING TRYPSIN INHIBITORS TO MAXIMIZE NUTRIENT UTILIZATION David Torres Sr. Regional Technical Services Lead - Minerals & Enzymes Novus 0.55 0.50 0.45 0.40 0.35 0.30 SBM TI, mg/g Pancreas Weight g/100 g of BW r2=0.989 0 2 4 6 8 10 12 14 Figure 1. Pancreas hypertrophy due to trypsin inhibitor1

RkJQdWJsaXNoZXIy MTUxNjkxNQ==