PT-010(PT-010) - 在研适应症：注意缺陷障碍伴多动_专利_临床

概要

基本信息

药物类型

小分子化药

别名

靶点-

作用机制-

治疗领域

其他疾病

在研适应症

注意缺陷障碍伴多动

非在研适应症-

原研机构

祐儿医药科技（上海）有限公司

在研机构

祐儿医药科技（上海）有限公司

非在研机构-

最高研发阶段批准上市

首次获批日期-

最高研发阶段(中国)临床前

特殊审评-

登录后查看时间轴

关联

100 项与 PT-010 相关的临床结果

登录后查看更多信息

100 项与 PT-010 相关的转化医学

登录后查看更多信息

100 项与 PT-010 相关的专利（医药）

登录后查看更多信息

1

项与 PT-010 相关的文献（医药）

2024-12-01·International Journal of Biological Macromolecules

Effect of limited hydrolysis on the structure and gel properties of soybean isolate proteins: A comparative study of papain or/and trypsin

Article

作者: Zhang, Shuang ; Li, Yang ; Xu, Bolin ; Zhang, Xiaoying ; Yin, Chengpeng ; Zhao, Qingkui

Plant protein's gelation is crucial in various food applications, and hydrolysis may enhance their gelation properties. In this study, we prepared soybean protein isolate hydrolysates (SPIH) using trypsin and/or papain, and found significant improvement in the solubility and gelling properties. These proteases broken down the peptide bonds and caused the exposure of hydrophobic groups as well as the unfolding of protein. Low molecular weight (<35 kDa) SPIHs were generated by the two-step enzymatic hydrolysis, showing significant improvements in storage modulus (G'), loss modulus (G″), viscosity, strength, and water-holding capacity (WHC). Among, PT-10 exhibited the highest WHC (61.72 ± 0.36 %), gel strength (4.67 ± 0.12 g), and network cross-linking density (0.33 ± 0.01 mol/m³), while its solubility was also significantly increased up to 254 %. According to the results of gel molecular force interactions, disulfide bonds, hydrophobic interactions and hydrogen bonds involved in the gel network formation. These findings reveal that the appropriate hydrolysis modification may improve SPI gel's properties and expand its application in gel foods.

100 项与 PT-010 相关的药物交易

登录后查看更多信息