Fat-soluble vitamin D is not classified as an essential nutrient because it can be made by the body during exposure of the skin to sun ultraviolet rays. 7-Dehydrocholesterol converts to previtamin D3 during exposure to ultraviolet radiation in the skin and then it is converted to vitamin D3 through thermal isomerization. Finally,vitamin D3 is hydroxylated to 25-hydroxyvitamin D (25-OHD) in the liver. Serum concentration of 25-OHD is considered as a clinical measure of vitamin D status (Wagner, Sidhom, Whiting, Rousseau, & Vieth, 2008).
One of the most important biological functions of vitamin D3 is to maintain blood calcium and phosphorus concentrations within a narrow physiological range (Forrest, Yada, & Rousseau, 2005). Recent evidence suggested that vitamin D has a protective effect against a variety of diseases, including multiple sclerosis (Kimball, Ursell, O'Connor, & Vieth, 2007; Mahon, Gordon, Cruz, Cosman, & Cantorna, 2003; Munger, Levin, Hollis, Howard, & Ascherio, 2006), diabetes (Casteels et al., 1998; Chiu, Chu, Go, & Saad, 2004; Hyppo€nen, L€aa€ra€, Reunanen, Ja€rvelin, & Virtanen, 2001), cardiovascular disease (Lind et al., 1995; Wang et al., 2008), mi- crobial infections (Liu et al., 2006; Martineau et al., 2007; Zasloff, 2006), metabolic syndrome, hypertension, bone diseases and cancer (Abbasi, Emam-Djomeh, Ebrahimzadeh Mousavi, & Davoodi, 2014; Forrest et al., 2005; Mocellin, 2011; Wagner et al., 2008).
Only a few foods contain vitamin D and often in very small amounts (Forrest et al., 2005; Holick, 1999). Fortified foods with this vitamin could be used to meet daily nutritional requirements of healthy consumer. Since hydrophobic compounds such as vitamin D are photosensitive, sensitive to pressure and oxidation as well as to adding to aqueous solutions, appropriate encapsulation method could be used to raise their stability and their bioavailability (Abbasi et al., 2014; Chen, Weiss, & Shahidi, 2006; Fessi, Puisieux, Devissaguet, Ammoury, & Benita, 1989; Ibrahim, Bindschaedler, Doelker, Buri, & Gurny, 1992). Biomacromolecules like proteins are good candidates for vitamin encapsulation. For example, beta- lactoglobulin and casein have been already used as nanovehicles for delivery of vitamin D2 and of docosahexaenoic acid. The use of proteins occuring naturally in dairy products will be inexpensive (Abbasi et al., 2014; Chatterton, Smithers, Roupas, & Brodkorb, 2006; Ha & Zemel, 2003). Milk proteins are divided into two frac- tions; caseins and whey proteins.
Whey proteins are globular proteins and constitute 20% of all milk proteins. Alpha-lactalbumin is one of them. Alpha- lactalbumin (a-La) is able to bind hydrophobic ligands such as retinol (Livney, 2010), hydrophobic column chromatography pha- ses, hydrophobic peptides, melittin of bee venom (Barbana et al., 2006), oleic acid (Gustafsson et al., 2005; Kehoe & Brodkorb, 2014). a-La is a small globular protein (123 amino acids) with a molecular mass of 14.2 kDa, acidic (pI 4.8 present in the milk of all mammals where it is involved in the synthesis of lactose. The concentration of a-La is 1e1.5 g/L in bovine milk (about 3.4% of total milk protein). Hence, it is one of a dominant protein in human milk (Jackson et al., 2004; Permyakov & Berliner, 2000). Natural struc- ture of bovine a-La consists of a large helical domain and a small beta-sheet domain, which is connected by a loop (Permyakov & Berliner, 2000). The helical domain contains three main alpha- helices (residues 5e11, 23e24 and 86e98) and two main smaller 310 helices (residue 18e20 and 115e118). The structure of beta sheet domain composes of three anti parallel beta strands (residue 41e44, 47e50 and 55e56), a 310 helix (residue 77e80) and some loops. The a-La has a deep cleft between two domains, four disul- fide bridges and one hydrophobic pocket. Native a-La contains a calcium ion, bound to its high affinity binding site in the loop connecting two domains. Depletion of calcium ion changes the a-La tertiary structure (Permyakov & Berliner, 2000). Research has shown that oleic acid and palmitic acid cannot be bound to holo a- La, but apo a-La has one binding site for oleic acid and another for palmitic acid (Cawthern, Narayan, Chaudhuri, Permyakov, & Berliner, 1997).
Food fortification with vitamin D can improve general health (Forrest et al., 2005; Holick, 1999). However, vitamin D is very sensitive to light, pressure and oxidation and to aqueous media (Abbasi et al., 2014; Chen et al., 2006; Fessi et al., 1989; Ibrahim et al., 1992). Previous studies have shown that enrichment of liquid milk alone is not enough and foods, except breast milk, should be supplemented with vitamin D3 (Holick, Shao, Liu, & Chen, 1992; Vieth, 1999; Vieth, Cole, Hawker, Trang, & Rubin, 2001). Enrichment of other dairy products, can compensate for the deficiency of vitamin D3 in consumed foods (McKenna et al., 1995). Some proteins such as casein and b-lactoglobulin were proposed as nanovehicles of vitamin D due to their low cost and availability (Forrest et al., 2005). In this paper, we investigated the interactions between vitamin D3 and apo a-La to examine suit- ability of a-La as a carrier of vitamin D3. a-La is a whey protein with the ability to interact with hydrophobic ligands. A study on vitamin D3 enriched cheddar cheese has shown that whey proteins loose
Fat-soluble vitamin D is not classified as an essential nutrient because it can be made by the body during exposure of the skin to sun ultraviolet rays. 7-Dehydrocholesterol converts to previtamin D3 during exposure to ultraviolet radiation in the skin and then it is converted to vitamin D3 through thermal isomerization. Finally,vitamin D3 is hydroxylated to 25-hydroxyvitamin D (25-OHD) in the liver. Serum concentration of 25-OHD is considered as a clinical measure of vitamin D status (Wagner, Sidhom, Whiting, Rousseau, & Vieth, 2008).One of the most important biological functions of vitamin D3 is to maintain blood calcium and phosphorus concentrations within a narrow physiological range (Forrest, Yada, & Rousseau, 2005). Recent evidence suggested that vitamin D has a protective effect against a variety of diseases, including multiple sclerosis (Kimball, Ursell, O'Connor, & Vieth, 2007; Mahon, Gordon, Cruz, Cosman, & Cantorna, 2003; Munger, Levin, Hollis, Howard, & Ascherio, 2006), diabetes (Casteels et al., 1998; Chiu, Chu, Go, & Saad, 2004; Hyppo€nen, L€aa€ra€, Reunanen, Ja€rvelin, & Virtanen, 2001), cardiovascular disease (Lind et al., 1995; Wang et al., 2008), mi- crobial infections (Liu et al., 2006; Martineau et al., 2007; Zasloff, 2006), metabolic syndrome, hypertension, bone diseases and cancer (Abbasi, Emam-Djomeh, Ebrahimzadeh Mousavi, & Davoodi, 2014; Forrest et al., 2005; Mocellin, 2011; Wagner et al., 2008).Only a few foods contain vitamin D and often in very small amounts (Forrest et al., 2005; Holick, 1999). Fortified foods with this vitamin could be used to meet daily nutritional requirements of healthy consumer. Since hydrophobic compounds such as vitamin D are photosensitive, sensitive to pressure and oxidation as well as to adding to aqueous solutions, appropriate encapsulation method could be used to raise their stability and their bioavailability (Abbasi et al., 2014; Chen, Weiss, & Shahidi, 2006; Fessi, Puisieux, Devissaguet, Ammoury, & Benita, 1989; Ibrahim, Bindschaedler, Doelker, Buri, & Gurny, 1992). Biomacromolecules like proteins are good candidates for vitamin encapsulation. For example, beta- lactoglobulin and casein have been already used as nanovehicles for delivery of vitamin D2 and of docosahexaenoic acid. The use of proteins occuring naturally in dairy products will be inexpensive (Abbasi et al., 2014; Chatterton, Smithers, Roupas, & Brodkorb, 2006; Ha & Zemel, 2003). Milk proteins are divided into two frac- tions; caseins and whey proteins.Whey proteins are globular proteins and constitute 20% of all milk proteins. Alpha-lactalbumin is one of them. Alpha- lactalbumin (a-La) is able to bind hydrophobic ligands such as retinol (Livney, 2010), hydrophobic column chromatography pha- ses, hydrophobic peptides, melittin of bee venom (Barbana et al., 2006), oleic acid (Gustafsson et al., 2005; Kehoe & Brodkorb, 2014). a-La is a small globular protein (123 amino acids) with a molecular mass of 14.2 kDa, acidic (pI 4.8 present in the milk of all mammals where it is involved in the synthesis of lactose. The concentration of a-La is 1e1.5 g/L in bovine milk (about 3.4% of total milk protein). Hence, it is one of a dominant protein in human milk (Jackson et al., 2004; Permyakov & Berliner, 2000). Natural struc- ture of bovine a-La consists of a large helical domain and a small beta-sheet domain, which is connected by a loop (Permyakov & Berliner, 2000). The helical domain contains three main alpha- helices (residues 5e11, 23e24 and 86e98) and two main smaller 310 helices (residue 18e20 and 115e118). The structure of beta sheet domain composes of three anti parallel beta strands (residue 41e44, 47e50 and 55e56), a 310 helix (residue 77e80) and some loops. The a-La has a deep cleft between two domains, four disul- fide bridges and one hydrophobic pocket. Native a-La contains a calcium ion, bound to its high affinity binding site in the loop connecting two domains. Depletion of calcium ion changes the a-La tertiary structure (Permyakov & Berliner, 2000). Research has shown that oleic acid and palmitic acid cannot be bound to holo a- La, but apo a-La has one binding site for oleic acid and another for palmitic acid (Cawthern, Narayan, Chaudhuri, Permyakov, & Berliner, 1997).Food fortification with vitamin D can improve general health (Forrest et al., 2005; Holick, 1999). However, vitamin D is very sensitive to light, pressure and oxidation and to aqueous media (Abbasi et al., 2014; Chen et al., 2006; Fessi et al., 1989; Ibrahim et al., 1992). Previous studies have shown that enrichment of liquid milk alone is not enough and foods, except breast milk, should be supplemented with vitamin D3 (Holick, Shao, Liu, & Chen, 1992; Vieth, 1999; Vieth, Cole, Hawker, Trang, & Rubin, 2001). Enrichment of other dairy products, can compensate for the deficiency of vitamin D3 in consumed foods (McKenna et al., 1995). Some proteins such as casein and b-lactoglobulin were proposed as nanovehicles of vitamin D due to their low cost and availability (Forrest et al., 2005). In this paper, we investigated the interactions between vitamin D3 and apo a-La to examine suit- ability of a-La as a carrier of vitamin D3. a-La is a whey protein with the ability to interact with hydrophobic ligands. A study on vitamin D3 enriched cheddar cheese has shown that whey proteins loose
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Fat-soluble vitamin D is not classified as an essential nutrient because it can be made by the body during exposure of the skin to sun ultraviolet rays. 7-Dehydrocholesterol converts to previtamin D3 during exposure to ultraviolet radiation in the skin and then it is converted to vitamin D3 through thermal isomerization. Finally,vitamin D3 is hydroxylated to 25-hydroxyvitamin D (25-OHD) in the liver. Serum concentration of 25-OHD is considered as a clinical measure of vitamin D status (Wagner, Sidhom, Whiting, Rousseau, & Vieth, 2008).
One of the most important biological functions of vitamin D3 is to maintain blood calcium and phosphorus concentrations within a narrow physiological range (Forrest, Yada, & Rousseau, 2005). Recent evidence suggested that vitamin D has a protective effect against a variety of diseases, including multiple sclerosis (Kimball, Ursell, O'Connor, & Vieth, 2007; Mahon, Gordon, Cruz, Cosman, & Cantorna, 2003; Munger, Levin, Hollis, Howard, & Ascherio, 2006), diabetes (Casteels et al., 1998; Chiu, Chu, Go, & Saad, 2004; Hyppo€nen, L€aa€ra€, Reunanen, Ja€rvelin, & Virtanen, 2001), cardiovascular disease (Lind et al., 1995; Wang et al., 2008), mi- crobial infections (Liu et al., 2006; Martineau et al., 2007; Zasloff, 2006), metabolic syndrome, hypertension, bone diseases and cancer (Abbasi, Emam-Djomeh, Ebrahimzadeh Mousavi, & Davoodi, 2014; Forrest et al., 2005; Mocellin, 2011; Wagner et al., 2008).
Only a few foods contain vitamin D and often in very small amounts (Forrest et al., 2005; Holick, 1999). Fortified foods with this vitamin could be used to meet daily nutritional requirements of healthy consumer. Since hydrophobic compounds such as vitamin D are photosensitive, sensitive to pressure and oxidation as well as to adding to aqueous solutions, appropriate encapsulation method could be used to raise their stability and their bioavailability (Abbasi et al., 2014; Chen, Weiss, & Shahidi, 2006; Fessi, Puisieux, Devissaguet, Ammoury, & Benita, 1989; Ibrahim, Bindschaedler, Doelker, Buri, & Gurny, 1992). Biomacromolecules like proteins are good candidates for vitamin encapsulation. For example, beta- lactoglobulin and casein have been already used as nanovehicles for delivery of vitamin D2 and of docosahexaenoic acid. The use of proteins occuring naturally in dairy products will be inexpensive (Abbasi et al., 2014; Chatterton, Smithers, Roupas, & Brodkorb, 2006; Ha & Zemel, 2003). Milk proteins are divided into two frac- tions; caseins and whey proteins.
Whey proteins are globular proteins and constitute 20% of all milk proteins. Alpha-lactalbumin is one of them. Alpha- lactalbumin (a-La) is able to bind hydrophobic ligands such as retinol (Livney, 2010), hydrophobic column chromatography pha- ses, hydrophobic peptides, melittin of bee venom (Barbana et al., 2006), oleic acid (Gustafsson et al., 2005; Kehoe & Brodkorb, 2014). a-La is a small globular protein (123 amino acids) with a molecular mass of 14.2 kDa, acidic (pI 4.8 present in the milk of all mammals where it is involved in the synthesis of lactose. The concentration of a-La is 1e1.5 g/L in bovine milk (about 3.4% of total milk protein). Hence, it is one of a dominant protein in human milk (Jackson et al., 2004; Permyakov & Berliner, 2000). Natural struc- ture of bovine a-La consists of a large helical domain and a small beta-sheet domain, which is connected by a loop (Permyakov & Berliner, 2000). The helical domain contains three main alpha- helices (residues 5e11, 23e24 and 86e98) and two main smaller 310 helices (residue 18e20 and 115e118). The structure of beta sheet domain composes of three anti parallel beta strands (residue 41e44, 47e50 and 55e56), a 310 helix (residue 77e80) and some loops. The a-La has a deep cleft between two domains, four disul- fide bridges and one hydrophobic pocket. Native a-La contains a calcium ion, bound to its high affinity binding site in the loop connecting two domains. Depletion of calcium ion changes the a-La tertiary structure (Permyakov & Berliner, 2000). Research has shown that oleic acid and palmitic acid cannot be bound to holo a- La, but apo a-La has one binding site for oleic acid and another for palmitic acid (Cawthern, Narayan, Chaudhuri, Permyakov, & Berliner, 1997).
Food fortification with vitamin D can improve general health (Forrest et al., 2005; Holick, 1999). However, vitamin D is very sensitive to light, pressure and oxidation and to aqueous media (Abbasi et al., 2014; Chen et al., 2006; Fessi et al., 1989; Ibrahim et al., 1992). Previous studies have shown that enrichment of liquid milk alone is not enough and foods, except breast milk, should be supplemented with vitamin D3 (Holick, Shao, Liu, & Chen, 1992; Vieth, 1999; Vieth, Cole, Hawker, Trang, & Rubin, 2001). Enrichment of other dairy products, can compensate for the deficiency of vitamin D3 in consumed foods (McKenna et al., 1995). Some proteins such as casein and b-lactoglobulin were proposed as nanovehicles of vitamin D due to their low cost and availability (Forrest et al., 2005). In this paper, we investigated the interactions between vitamin D3 and apo a-La to examine suit- ability of a-La as a carrier of vitamin D3. a-La is a whey protein with the ability to interact with hydrophobic ligands. A study on vitamin D3 enriched cheddar cheese has shown that whey proteins loose
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ละลายไขมันวิตามิน D ไม่จัดเป็นสารอาหารจำเป็น เพราะมันสามารถทำได้โดยร่างกายในการเปิดรับแสงของผิวดวงอาทิตย์รังสีอัลตราไวโอเลต . 7-dehydrocholesterol แปลง previtamin D3 ในการสัมผัสกับรังสีอัลตราไวโอเลตในผิวแล้วมันแปลงเป็นวิตามิน D3 ผ่านความร้อนไอโซเมอไรเซชัน . ในที่สุดวิตามิน D3 เป็น hydroxylated 25 hydroxyvitamin D ( 25-ohd ) ในตับ เซรั่มเข้มข้น 25-ohd ถือว่าเป็นตัวชี้วัดทางคลินิกของวิตามินดี สถานะ ( วากเนอร์ sidhom Whiting , Rousseau , & vieth , 2008 ) .
อย่างใดอย่างหนึ่งของฟังก์ชันทางชีวภาพที่สำคัญที่สุดของวิตามิน D3 เพื่อรักษาระดับแคลเซียมในเลือด และปริมาณฟอสฟอรัสในช่วงแคบทางสรีรวิทยา ( ฟอเรสท์ ยาดา &รุสโซ่2005 ) หลักฐานล่าสุดพบว่าวิตามิน D มีผลป้องกันความหลากหลายของโรค ได้แก่ โรคปลอกประสาทอักเสบ ( ursell คิมบอลล์ , , โอคอนเนอร์ , & vieth , 2007 ; เมเอิ้น กอร์ดอน ครูซ , Cosman & cantorna , 2003 ; มังเกอร์ , เลวิน ฮอลลิส ฮาเวิร์ด & ascherio , 2006 ) , เบาหวาน ( casteels et al . , 1998 ; ชิว ชู ไป & Saad , 2004 ; hyppo ดเณร ผมแคร์แคร์แคร์ reunanen รา AA , , และด้าน rvelin &เวอทาเน่น , ,2001 ) , โรคหัวใจและหลอดเลือด ( ลินด์ et al . , 1995 ; Wang et al . , 2008 ) , มิ - เชื้อ crobial ( Liu et al . , 2006 ; มาร์ติโน่ et al . , 2007 ; zasloff , 2006 ) , โรคเมตาบอลิ , ความดันโลหิตสูง , โรคกระดูกและมะเร็ง ( Abbasi emam djomeh , ebrahimzadeh Mousavi & , , davoodi 2014 ; Forrest et al . , 2005 ; mocellin 2011 ; วากเนอร์ et al . , 2008 ) .
เพียงไม่กี่อาหารที่ประกอบด้วยวิตามิน D และมักจะในปริมาณที่น้อยมาก ( Forrest et al . , 2005 ; Holick , 1999 ) เสริมอาหารที่มีวิตามินนี้สามารถใช้เพื่อตอบสนองความต้องการทางโภชนาการของผู้บริโภคทุกวัน สุขภาพแข็งแรง เนื่องจากสาร hydrophobic เช่นวิตามิน D แสง , ไวต่อความดันและออกซิเจน รวมทั้งเพิ่มสารละลายน้ำวิธีการที่เหมาะสมสามารถใช้เพื่อเพิ่มความมั่นคงของพวกเขาและการดูดซึมของพวกเขา ( Abbasi et al . , 2014 ; เฉิน ไวส์ & shahidi , 2006 ; fessi puisieux devissaguet ammoury , , , , &เบนิต้า , 1989 ; อิบราฮิม bindschaedler doelker บุรี , & gurny , 2535 ) biomacromolecules เช่นโปรตีนมีผู้สมัครที่ดีสำหรับการวิตามิน . ตัวอย่างเช่นเบต้า - แลคโตกลอบูลินเคซีนและได้ถูกใช้ไปแล้วเป็น nanovehicles ส่งมอบวิตามิน D2 และ docosahexaenoic acid . การใช้โปรตีนที่มีอยู่ตามธรรมชาติในนมจะไม่แพง ( Abbasi et al . , 2014 ; แชตเตอร์ตันสมิทเทอร์ส roupas & , , , brodkorb , 2006 ; ฮา&เซเมล , 2003 ) โปรตีนในนมจะถูกแบ่งออกเป็นสองใช้งาน frac - ; โปรตีนสารเคซีนและโปรตีน .
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