ฉันรักการแปลIn this study, we inves

ฉันรักการแปลIn this study, we investigated the interaction of Vaccinium bracteatum Thunb. leaf (VBTL) pigment and
rice proteins. In the presence of rice protein, VBTL pigment antioxidant activity and free polyphenol content
decreased by 67.19% and 68.11%, respectively, and L* of the protein–pigment complex decreased significantly
over time. L* values of albumin, globulin and glutelin during 60-min pigment exposure
decreased by 55.00, 57.14, and 54.30%, respectively, indicating that these proteins had bound to the pigment.
A significant difference in protein surface hydrophobicity was observed between rice proteins and
pigment–protein complexes, indicating that hydrophobic interaction is a major binding mechanism
between VBTL pigment and rice proteins. A significant difference in secondary structures between proteins
and protein–pigment complexes was also uncovered, indicating that hydrogen bonding may be
another mode of interaction between VBTL pigment and rice proteins. Our results indicate that VBTL pigment
can stain rice proteins with hydrophobic and hydrogen interactions.

2015 Elsevie

ผลลัพธ์ (อังกฤษ) 1:

I love In this study, we translated the Vaccinium bracteatum Thunb investigated interaction of leaf (VBTL) and pigment.rice proteins. In the presence of rice protein, VBTL pigment antioxidant activity and free polyphenol contentdecreased by 67.19% and 68.11%, respectively, and L* of the protein–pigment complex decreased significantlyover time. L* values of albumin, globulin and glutelin during 60-min pigment exposuredecreased by 55.00, 57.14, and 54.30%, respectively, indicating that these proteins had bound to the pigment.A significant difference in protein surface hydrophobicity was observed between rice proteins andpigment–protein complexes, indicating that hydrophobic interaction is a major binding mechanismbetween VBTL pigment and rice proteins. A significant difference in secondary structures between proteinsand protein–pigment complexes was also uncovered, indicating that hydrogen bonding may beanother mode of interaction between VBTL pigment and rice proteins. Our results indicate that VBTL pigmentcan stain rice proteins with hydrophobic and hydrogen interactions.2015 Elsevie

ผลลัพธ์ (อังกฤษ) 2:

I love to translate In this Study, we investigated the Interaction of Vaccinium bracteatum Thunb. Leaf (VBTL) pigment and
Rice Proteins. In the Presence of Rice protein, VBTL pigment antioxidant Activity and free polyphenol content
Decreased by 67.19% and 68.11%, respectively. , and L * of the protein-pigment Complex Decreased significantly
over time. L * values ​​of albumin, globulin and Glutelin during 60-min pigment exposure
Decreased by 55.00, 57.14, and 54.30%, respectively, Indicating that these Proteins had bound to the. pigment.
A significant difference in protein surface hydrophobicity was observed between Rice Proteins and
pigment-protein complexes, Indicating that hydrophobic Interaction is a Major binding mechanism
between VBTL pigment and Rice Proteins. A significant difference in Secondary Structures between Proteins
and protein-pigment complexes was. also Uncovered, Indicating that hydrogen bonding May be
another mode of Interaction between VBTL pigment and Rice Proteins. Our results indicate that pigment VBTL
Rice Proteins Can stain with hydrogen and hydrophobic interactions.
? 2015th Elsevie.

ผลลัพธ์ (อังกฤษ) 3:

I love In translation, this study we investigated the interaction of Vaccinium bracteatum Thunb. Leaf (VBTL) pigment and
rice. Proteins. In the presence of rice protein VBTL pigment, antioxidant activity and free polyphenol content
decreased by 67.19% and 68.11% respectively,,, And L * of the protein - pigment complex decreased significantly
over time. L * values, of albuminGlobulin and glutelin during 60-min pigment exposure
decreased by 55.00 57.14 and 54.30% respectively,,,,, indicating that These proteins had bound to the pigment.
A significant difference in protein surface hydrophobicity was observed between. Rice proteins and
pigment - protein complexes indicating that, hydrophobic interaction is a major binding mechanism
between. VBTL pigment and rice proteins.A significant difference in secondary structures between proteins
and protein - pigment complexes was, also uncovered indicating. That hydrogen bonding may be
another mode of interaction between VBTL pigment and rice proteins. Our results indicate that. VBTL pigment
can stain rice proteins with hydrophobic and hydrogen
2015 Elsevie interactions.

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