与马蛋白分离物中的酶活性相关的帕他丁和氧基酶变体概况
Thore H Diefenbach1, Gijs J C Vreeke1, Robin E J Spelbrink2
1Laboratory of Food Chemistry, Wageningen University, Bornse Weilanden 9, 6708, WG, Wageningen, the Netherlands.
Food chemistry
|March 5, 2025
概括
像脂酶和脂氧酶这样的土豆酶会在蛋白质分离物中引起异味. 不同的土豆品种之间的酶活性差异并不能用遗传变异或翻译后修改来解释.
科学领域:
- 食品科学 食品科学 食品科学
- 生物化学 生物化学
- 植物科学 植物科学
背景情况:
- 马蛋白分离物中的脂酶和脂氧酶有助于产生不良的味道,限制了它们在食品中的使用.
- 在土豆品种之间存在酶活性的显著差异,即使加工和蛋白质含量相似.
研究的目的:
- 研究遗传变异,翻译后修饰 (糖化和化) 以及土豆蛋白分离物中脂酶和脂氧酶的活动之间的关系.
- 了解不同种类的土豆种类中酶活性变化的原因.
主要方法:
- 从八种土豆品种中提取的蛋白质提取物被分析为脂酶和脂氧基酶活动.
- 超高性能液态染色学-质谱学 (UHPLC-MS) 用于检查变异形状.
- 评估了目标酶的糖化和化水平.
主要成果:
- 在不同品种中,脂酶和脂氧酶活性显著变化 (分别是十倍和四倍).
- 在变异形状和酶活性水平之间没有观察到相关性.
- 脂酶变体被持续地糖化,但没有被化;脂氧基酶变体没有显示任何翻译后的修改.
结论:
- 在土豆品种之间观察到的脂酶和脂氧酶活动的差异不能归因于它们的遗传变异概况或它们的糖化/酸化状态的变化.
- 需要进一步的研究来确定其他影响土豆蛋白分离物的酶活性的因素.
相关概念视频
Enzymes
Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
Protein Kinases and Phosphatases
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Detergent Purification of Membrane Proteins
Detergents are used to purify the integral proteins of the membrane. The hydrophobic portion of the detergent can replace membrane phospholipids while solubilizing the membrane proteins. When detergent monomers reach a specific concentration in a solution called critical micelle concentration (CMC), they form micelles. Above CMC, the concentration of the detergent monomers remains in equilibrium with the micelle. The number of detergent monomers present in the CMC varies for each detergent, and...
Introduction to Mechanisms of Enzyme Catalysis
For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...
SDS-PAGE
Gel electrophoresis is a method that separates biological macromolecules like nucleic acids or proteins by forcing them to pass through a gel matrix under an electric field.
A variation of gel electrophoresis, termed polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact proteins...
A variation of gel electrophoresis, termed polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact proteins...
Protein Denaturation
The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...


