- Teks
- Sejarah
fruits and vegetables. In many huma
fruits and vegetables. In many humans, absence of or too little of an enzyme is responsible for many genetically related diseases
[104].
Microbially caused diseases present another problem. The best way to treat these types of diseases is through inhibition of one
or more key enzymes of the microorganisms, resulting in their death. The inhibitors might compete reversibly with substrates or
cofactors for binding to the active site, or the inhibitor might form a covalent bond with active site groups (affinity labeling
inhibitor), or the compound might be treated as a substrate and be catalyzed to a product that, while still in the active site, forms
a convalent bond with a group in the active site (
k
cat inhibitors) [8]. The last type is the most specific and desirable in medicine
and in food because the inhibitor can be targeted specifically for the enzyme.
Enzymes continue to catalyze reactions in raw food materials after they reach maturity. These reactions can lead to loss of color,
texture, flavor and aroma, and nutritional quality. Therefore, there is need for control of these enzymes to stabilize the product as
food. Enzyme inhibitors are also important in the control of insects and microorganisms that attack raw food. They also are used
as herbicides in the control of unwanted weeds, grasses, and shrubs.
Enzyme inhibitors are an important means of controlling enzyme activity. An enzyme inhibitors is any compound that decreases
v
o when added to the enzyme-substrate reaction. There are many enzyme inhibitors, both naturally occurring and synthetic
[106]. Some inhibitors bind reversibly to enzymes and others form irreversible, covalent bonds with the enzymes. Some
inhibitors are large proteins or carbohydrates, and others are as small as HCN. Products of enzyme-catalyzed reactions can be
inhibitory.
Change in pH can alter activity by making conditions less optimum for enzyme activity. Elevated temperatures can decrease
enzyme activity by denaturing some of the enzyme, but at the same time increasing the velocity of conversion of substrate to
product by the active enzyme. Most enzymologists do not consider either of these variables to be enzyme inhibitors.
Denaturation of the enzyme eliminates its activity, and this can be accomplished by shear forces, very high pressures, irradiation,
or miscible organic solvents. Enzyme activity can also be decreased by chemical modification of essential active site groups of
the enzyme. Enzymes are also inactive when their substrate(s) are removed. All of these inhibitory approaches are valid ways of
controlling enzyme activities in foods.
7.7.1 Reversible Inhibitors
Reversible inhibitors are distinguished from irreversible inhibitors by the following criteria: (a) reversible inhibitors rapidly (within
milliseconds) form noncovalent diffusion-controlled equilibrium complexes with enzymes; the complex can be dissociated and
enzyme activity restored by displacing the equilibrium by dialysis or by gel filtration; (b) irreversible inhibitors slowly form
covalent derivatives of the enzyme that cannot be dissociated by dialysis or by gel filtration.
The reversible inhibitors can be treated kinetically by the methods described in Section 7.4 provided the equilibrium dissociation
constant (
K
i) is not less then 10
M.
Four types of reversible inhibitors can be identified based on their effects on the slopes and
intercepts of Lineweaver-Burk plots,
V
max and
K
m, or allosteric effects: (a) competitive inhibitors, (b) noncompetitive inhibitors,
(c) uncompetitive inhibitors, and (d) allosteric inhibitors. Allosteric #inhibitors not only decrease the velocity of the enzymecatalyzed
reactions, they cause allosteric (sigmoidal) plots of
v
o
versus [I], similar to the effect of [S]o
(Fig. 11).
-8
The type of reversible inhibitor must be determined by kinetic methods. Fortunately, all the mathematical equations differ in slope
and/or
y
-intercept only by 1 + [I]o/
K
i from the Michaelis-Menten and Lineweaver-Burk equations in the absence of inhibitor.
[104].
Microbially caused diseases present another problem. The best way to treat these types of diseases is through inhibition of one
or more key enzymes of the microorganisms, resulting in their death. The inhibitors might compete reversibly with substrates or
cofactors for binding to the active site, or the inhibitor might form a covalent bond with active site groups (affinity labeling
inhibitor), or the compound might be treated as a substrate and be catalyzed to a product that, while still in the active site, forms
a convalent bond with a group in the active site (
k
cat inhibitors) [8]. The last type is the most specific and desirable in medicine
and in food because the inhibitor can be targeted specifically for the enzyme.
Enzymes continue to catalyze reactions in raw food materials after they reach maturity. These reactions can lead to loss of color,
texture, flavor and aroma, and nutritional quality. Therefore, there is need for control of these enzymes to stabilize the product as
food. Enzyme inhibitors are also important in the control of insects and microorganisms that attack raw food. They also are used
as herbicides in the control of unwanted weeds, grasses, and shrubs.
Enzyme inhibitors are an important means of controlling enzyme activity. An enzyme inhibitors is any compound that decreases
v
o when added to the enzyme-substrate reaction. There are many enzyme inhibitors, both naturally occurring and synthetic
[106]. Some inhibitors bind reversibly to enzymes and others form irreversible, covalent bonds with the enzymes. Some
inhibitors are large proteins or carbohydrates, and others are as small as HCN. Products of enzyme-catalyzed reactions can be
inhibitory.
Change in pH can alter activity by making conditions less optimum for enzyme activity. Elevated temperatures can decrease
enzyme activity by denaturing some of the enzyme, but at the same time increasing the velocity of conversion of substrate to
product by the active enzyme. Most enzymologists do not consider either of these variables to be enzyme inhibitors.
Denaturation of the enzyme eliminates its activity, and this can be accomplished by shear forces, very high pressures, irradiation,
or miscible organic solvents. Enzyme activity can also be decreased by chemical modification of essential active site groups of
the enzyme. Enzymes are also inactive when their substrate(s) are removed. All of these inhibitory approaches are valid ways of
controlling enzyme activities in foods.
7.7.1 Reversible Inhibitors
Reversible inhibitors are distinguished from irreversible inhibitors by the following criteria: (a) reversible inhibitors rapidly (within
milliseconds) form noncovalent diffusion-controlled equilibrium complexes with enzymes; the complex can be dissociated and
enzyme activity restored by displacing the equilibrium by dialysis or by gel filtration; (b) irreversible inhibitors slowly form
covalent derivatives of the enzyme that cannot be dissociated by dialysis or by gel filtration.
The reversible inhibitors can be treated kinetically by the methods described in Section 7.4 provided the equilibrium dissociation
constant (
K
i) is not less then 10
M.
Four types of reversible inhibitors can be identified based on their effects on the slopes and
intercepts of Lineweaver-Burk plots,
V
max and
K
m, or allosteric effects: (a) competitive inhibitors, (b) noncompetitive inhibitors,
(c) uncompetitive inhibitors, and (d) allosteric inhibitors. Allosteric #inhibitors not only decrease the velocity of the enzymecatalyzed
reactions, they cause allosteric (sigmoidal) plots of
v
o
versus [I], similar to the effect of [S]o
(Fig. 11).
-8
The type of reversible inhibitor must be determined by kinetic methods. Fortunately, all the mathematical equations differ in slope
and/or
y
-intercept only by 1 + [I]o/
K
i from the Michaelis-Menten and Lineweaver-Burk equations in the absence of inhibitor.
0/5000
fruits and vegetables. In many humans, absence of or too little of an enzyme is responsible for many genetically related diseases
[104].
Microbially caused diseases present another problem. The best way to treat these types of diseases is through inhibition of one
or more key enzymes of the microorganisms, resulting in their death. The inhibitors might compete reversibly with substrates or
cofactors for binding to the active site, or the inhibitor might form a covalent bond with active site groups (affinity labeling
inhibitor), or the compound might be treated as a substrate and be catalyzed to a product that, while still in the active site, forms
a convalent bond with a group in the active site (
k
cat inhibitors) [8]. The last type is the most specific and desirable in medicine
and in food because the inhibitor can be targeted specifically for the enzyme.
Enzymes continue to catalyze reactions in raw food materials after they reach maturity. These reactions can lead to loss of color,
texture, flavor and aroma, and nutritional quality. Therefore, there is need for control of these enzymes to stabilize the product as
food. Enzyme inhibitors are also important in the control of insects and microorganisms that attack raw food. They also are used
as herbicides in the control of unwanted weeds, grasses, and shrubs.
Enzyme inhibitors are an important means of controlling enzyme activity. An enzyme inhibitors is any compound that decreases
v
o when added to the enzyme-substrate reaction. There are many enzyme inhibitors, both naturally occurring and synthetic
[106]. Some inhibitors bind reversibly to enzymes and others form irreversible, covalent bonds with the enzymes. Some
inhibitors are large proteins or carbohydrates, and others are as small as HCN. Products of enzyme-catalyzed reactions can be
inhibitory.
Change in pH can alter activity by making conditions less optimum for enzyme activity. Elevated temperatures can decrease
enzyme activity by denaturing some of the enzyme, but at the same time increasing the velocity of conversion of substrate to
product by the active enzyme. Most enzymologists do not consider either of these variables to be enzyme inhibitors.
Denaturation of the enzyme eliminates its activity, and this can be accomplished by shear forces, very high pressures, irradiation,
or miscible organic solvents. Enzyme activity can also be decreased by chemical modification of essential active site groups of
the enzyme. Enzymes are also inactive when their substrate(s) are removed. All of these inhibitory approaches are valid ways of
controlling enzyme activities in foods.
7.7.1 Reversible Inhibitors
Reversible inhibitors are distinguished from irreversible inhibitors by the following criteria: (a) reversible inhibitors rapidly (within
milliseconds) form noncovalent diffusion-controlled equilibrium complexes with enzymes; the complex can be dissociated and
enzyme activity restored by displacing the equilibrium by dialysis or by gel filtration; (b) irreversible inhibitors slowly form
covalent derivatives of the enzyme that cannot be dissociated by dialysis or by gel filtration.
The reversible inhibitors can be treated kinetically by the methods described in Section 7.4 provided the equilibrium dissociation
constant (
K
i) is not less then 10
M.
Four types of reversible inhibitors can be identified based on their effects on the slopes and
intercepts of Lineweaver-Burk plots,
V
max and
K
m, or allosteric effects: (a) competitive inhibitors, (b) noncompetitive inhibitors,
(c) uncompetitive inhibitors, and (d) allosteric inhibitors. Allosteric #inhibitors not only decrease the velocity of the enzymecatalyzed
reactions, they cause allosteric (sigmoidal) plots of
v
o
versus [I], similar to the effect of [S]o
(Fig. 11).
-8
The type of reversible inhibitor must be determined by kinetic methods. Fortunately, all the mathematical equations differ in slope
and/or
y
-intercept only by 1 + [I]o/
K
i from the Michaelis-Menten and Lineweaver-Burk equations in the absence of inhibitor.
[104].
Microbially caused diseases present another problem. The best way to treat these types of diseases is through inhibition of one
or more key enzymes of the microorganisms, resulting in their death. The inhibitors might compete reversibly with substrates or
cofactors for binding to the active site, or the inhibitor might form a covalent bond with active site groups (affinity labeling
inhibitor), or the compound might be treated as a substrate and be catalyzed to a product that, while still in the active site, forms
a convalent bond with a group in the active site (
k
cat inhibitors) [8]. The last type is the most specific and desirable in medicine
and in food because the inhibitor can be targeted specifically for the enzyme.
Enzymes continue to catalyze reactions in raw food materials after they reach maturity. These reactions can lead to loss of color,
texture, flavor and aroma, and nutritional quality. Therefore, there is need for control of these enzymes to stabilize the product as
food. Enzyme inhibitors are also important in the control of insects and microorganisms that attack raw food. They also are used
as herbicides in the control of unwanted weeds, grasses, and shrubs.
Enzyme inhibitors are an important means of controlling enzyme activity. An enzyme inhibitors is any compound that decreases
v
o when added to the enzyme-substrate reaction. There are many enzyme inhibitors, both naturally occurring and synthetic
[106]. Some inhibitors bind reversibly to enzymes and others form irreversible, covalent bonds with the enzymes. Some
inhibitors are large proteins or carbohydrates, and others are as small as HCN. Products of enzyme-catalyzed reactions can be
inhibitory.
Change in pH can alter activity by making conditions less optimum for enzyme activity. Elevated temperatures can decrease
enzyme activity by denaturing some of the enzyme, but at the same time increasing the velocity of conversion of substrate to
product by the active enzyme. Most enzymologists do not consider either of these variables to be enzyme inhibitors.
Denaturation of the enzyme eliminates its activity, and this can be accomplished by shear forces, very high pressures, irradiation,
or miscible organic solvents. Enzyme activity can also be decreased by chemical modification of essential active site groups of
the enzyme. Enzymes are also inactive when their substrate(s) are removed. All of these inhibitory approaches are valid ways of
controlling enzyme activities in foods.
7.7.1 Reversible Inhibitors
Reversible inhibitors are distinguished from irreversible inhibitors by the following criteria: (a) reversible inhibitors rapidly (within
milliseconds) form noncovalent diffusion-controlled equilibrium complexes with enzymes; the complex can be dissociated and
enzyme activity restored by displacing the equilibrium by dialysis or by gel filtration; (b) irreversible inhibitors slowly form
covalent derivatives of the enzyme that cannot be dissociated by dialysis or by gel filtration.
The reversible inhibitors can be treated kinetically by the methods described in Section 7.4 provided the equilibrium dissociation
constant (
K
i) is not less then 10
M.
Four types of reversible inhibitors can be identified based on their effects on the slopes and
intercepts of Lineweaver-Burk plots,
V
max and
K
m, or allosteric effects: (a) competitive inhibitors, (b) noncompetitive inhibitors,
(c) uncompetitive inhibitors, and (d) allosteric inhibitors. Allosteric #inhibitors not only decrease the velocity of the enzymecatalyzed
reactions, they cause allosteric (sigmoidal) plots of
v
o
versus [I], similar to the effect of [S]o
(Fig. 11).
-8
The type of reversible inhibitor must be determined by kinetic methods. Fortunately, all the mathematical equations differ in slope
and/or
y
-intercept only by 1 + [I]o/
K
i from the Michaelis-Menten and Lineweaver-Burk equations in the absence of inhibitor.
Sedang diterjemahkan, harap tunggu..
buah-buahan dan sayuran. Dalam banyak manusia, tidak adanya atau terlalu sedikit enzim yang bertanggung jawab untuk banyak penyakit yang berhubungan secara genetis
[104].
Microbially menyebabkan penyakit ini masalah lain. Cara terbaik untuk mengobati jenis penyakit adalah melalui penghambatan satu
atau lebih enzim kunci dari mikroorganisme, sehingga kematian mereka. Inhibitor mungkin bersaing reversibel dengan substrat atau
kofaktor untuk mengikat ke situs aktif, atau inhibitor mungkin membentuk ikatan kovalen dengan kelompok situs aktif (afinitas label
inhibitor), atau senyawa yang mungkin diperlakukan sebagai substrat dan dikatalisasi dengan produk yang , sementara masih dalam situs aktif, membentuk
ikatan convalent dengan kelompok di situs aktif (
k
inhibitor kucing) [8]. Jenis terakhir adalah yang paling spesifik dan diinginkan dalam pengobatan
dan makanan karena inhibitor dapat ditargetkan khusus untuk enzim.
Enzim terus mengkatalisis reaksi bahan makanan mentah setelah mereka mencapai kematangan. Reaksi-reaksi ini dapat menyebabkan hilangnya warna,
tekstur, rasa dan aroma, dan kualitas gizi. Oleh karena itu, ada kebutuhan untuk kontrol enzim ini untuk menstabilkan produk sebagai
makanan. Inhibitor enzim juga penting dalam pengendalian serangga dan mikroorganisme yang menyerang makanan mentah. Mereka juga digunakan
sebagai herbisida dalam pengendalian gulma yang tidak diinginkan, rumput, dan semak belukar.
inhibitor enzim merupakan sarana penting untuk mengontrol aktivitas enzim. Sebuah inhibitor enzim adalah senyawa yang menurunkan
v
o ketika ditambahkan ke reaksi enzim-substrat. Ada banyak inhibitor enzim, baik alami dan sintetis
[106]. Beberapa inhibitor mengikat reversibel enzim dan lain-lain membentuk ireversibel, ikatan kovalen dengan enzim. Beberapa
inhibitor protein besar atau karbohidrat, dan lain-lain sekecil HCN. Produk reaksi enzim-dikatalisasi bisa
penghambatan.
Perubahan pH dapat mengubah aktivitas dengan membuat kondisi yang kurang optimal untuk aktivitas enzim. Suhu yang tinggi dapat menurunkan
aktivitas enzim dengan denaturasi beberapa enzim, tetapi pada saat yang sama meningkatkan kecepatan konversi substrat untuk
produk dengan enzim aktif. Kebanyakan enzymologists tidak menganggap salah satu dari variabel-variabel ini menjadi penghambat enzim.
Denaturasi enzim menghilangkan aktivitas, dan hal ini dapat dicapai dengan gaya geser, tekanan yang sangat tinggi, iradiasi,
atau pelarut organik larut. Aktivitas enzim juga dapat dikurangi dengan modifikasi kimia kelompok situs aktif penting dari
enzim. Enzim juga aktif ketika substrat mereka (s) akan dihapus. Semua pendekatan penghambatan cara yang sah
mengendalikan aktivitas enzim dalam makanan.
7.7.1 Inhibitor Reversible
inhibitor Reversible dibedakan dari inhibitor ireversibel dengan kriteria sebagai berikut: (a) inhibitor reversibel cepat (dalam
milidetik) membentuk kompleks keseimbangan difusi-dikendalikan noncovalent dengan enzim; kompleks dapat dipisahkan dan
aktivitas enzim dipulihkan oleh menggusur keseimbangan dengan dialisis atau filtrasi gel; (B) inhibitor ireversibel perlahan membentuk
turunan kovalen enzim yang tidak dapat dipisahkan dengan dialisis atau filtrasi gel.
Penghambat reversibel dapat diobati secara kinetik oleh metode yang dijelaskan dalam Bagian 7.4 memberikan kesetimbangan disosiasi
konstan (
K
i) tidak kurang 10 M. Empat jenis inhibitor reversibel dapat diidentifikasi berdasarkan efek mereka di lereng dan penyadapan dari Lineweaver-Burk plot, V max dan K m, atau efek alosterik: (a) inhibitor kompetitif, (b) inhibitor nonkompetitif, (c ) inhibitor kompetitif, dan (d) inhibitor alosterik. #inhibitors Alosterik tidak hanya mengurangi kecepatan dari enzymecatalyzed reaksi, mereka menyebabkan alosterik (sigmoidal) bidang v o dibandingkan [I], mirip dengan efek dari [S] o (Gambar. 11). -8 Jenis inhibitor reversibel harus ditentukan dengan metode kinetik. Untungnya, semua persamaan matematika berbeda dalam kemiringan dan / atau y -intercept hanya dengan 1 + [I] o / K i dari persamaan Michaelis Menten dan Lineweaver-Burk tanpa adanya inhibitor.
[104].
Microbially menyebabkan penyakit ini masalah lain. Cara terbaik untuk mengobati jenis penyakit adalah melalui penghambatan satu
atau lebih enzim kunci dari mikroorganisme, sehingga kematian mereka. Inhibitor mungkin bersaing reversibel dengan substrat atau
kofaktor untuk mengikat ke situs aktif, atau inhibitor mungkin membentuk ikatan kovalen dengan kelompok situs aktif (afinitas label
inhibitor), atau senyawa yang mungkin diperlakukan sebagai substrat dan dikatalisasi dengan produk yang , sementara masih dalam situs aktif, membentuk
ikatan convalent dengan kelompok di situs aktif (
k
inhibitor kucing) [8]. Jenis terakhir adalah yang paling spesifik dan diinginkan dalam pengobatan
dan makanan karena inhibitor dapat ditargetkan khusus untuk enzim.
Enzim terus mengkatalisis reaksi bahan makanan mentah setelah mereka mencapai kematangan. Reaksi-reaksi ini dapat menyebabkan hilangnya warna,
tekstur, rasa dan aroma, dan kualitas gizi. Oleh karena itu, ada kebutuhan untuk kontrol enzim ini untuk menstabilkan produk sebagai
makanan. Inhibitor enzim juga penting dalam pengendalian serangga dan mikroorganisme yang menyerang makanan mentah. Mereka juga digunakan
sebagai herbisida dalam pengendalian gulma yang tidak diinginkan, rumput, dan semak belukar.
inhibitor enzim merupakan sarana penting untuk mengontrol aktivitas enzim. Sebuah inhibitor enzim adalah senyawa yang menurunkan
v
o ketika ditambahkan ke reaksi enzim-substrat. Ada banyak inhibitor enzim, baik alami dan sintetis
[106]. Beberapa inhibitor mengikat reversibel enzim dan lain-lain membentuk ireversibel, ikatan kovalen dengan enzim. Beberapa
inhibitor protein besar atau karbohidrat, dan lain-lain sekecil HCN. Produk reaksi enzim-dikatalisasi bisa
penghambatan.
Perubahan pH dapat mengubah aktivitas dengan membuat kondisi yang kurang optimal untuk aktivitas enzim. Suhu yang tinggi dapat menurunkan
aktivitas enzim dengan denaturasi beberapa enzim, tetapi pada saat yang sama meningkatkan kecepatan konversi substrat untuk
produk dengan enzim aktif. Kebanyakan enzymologists tidak menganggap salah satu dari variabel-variabel ini menjadi penghambat enzim.
Denaturasi enzim menghilangkan aktivitas, dan hal ini dapat dicapai dengan gaya geser, tekanan yang sangat tinggi, iradiasi,
atau pelarut organik larut. Aktivitas enzim juga dapat dikurangi dengan modifikasi kimia kelompok situs aktif penting dari
enzim. Enzim juga aktif ketika substrat mereka (s) akan dihapus. Semua pendekatan penghambatan cara yang sah
mengendalikan aktivitas enzim dalam makanan.
7.7.1 Inhibitor Reversible
inhibitor Reversible dibedakan dari inhibitor ireversibel dengan kriteria sebagai berikut: (a) inhibitor reversibel cepat (dalam
milidetik) membentuk kompleks keseimbangan difusi-dikendalikan noncovalent dengan enzim; kompleks dapat dipisahkan dan
aktivitas enzim dipulihkan oleh menggusur keseimbangan dengan dialisis atau filtrasi gel; (B) inhibitor ireversibel perlahan membentuk
turunan kovalen enzim yang tidak dapat dipisahkan dengan dialisis atau filtrasi gel.
Penghambat reversibel dapat diobati secara kinetik oleh metode yang dijelaskan dalam Bagian 7.4 memberikan kesetimbangan disosiasi
konstan (
K
i) tidak kurang 10 M. Empat jenis inhibitor reversibel dapat diidentifikasi berdasarkan efek mereka di lereng dan penyadapan dari Lineweaver-Burk plot, V max dan K m, atau efek alosterik: (a) inhibitor kompetitif, (b) inhibitor nonkompetitif, (c ) inhibitor kompetitif, dan (d) inhibitor alosterik. #inhibitors Alosterik tidak hanya mengurangi kecepatan dari enzymecatalyzed reaksi, mereka menyebabkan alosterik (sigmoidal) bidang v o dibandingkan [I], mirip dengan efek dari [S] o (Gambar. 11). -8 Jenis inhibitor reversibel harus ditentukan dengan metode kinetik. Untungnya, semua persamaan matematika berbeda dalam kemiringan dan / atau y -intercept hanya dengan 1 + [I] o / K i dari persamaan Michaelis Menten dan Lineweaver-Burk tanpa adanya inhibitor.
Sedang diterjemahkan, harap tunggu..
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- Mengikhkaskan demi sesuatu yang baik
- Manusia tidak ada yang sempurna..hidup a
- Mengikhlaskan demi sesuatu yang baik
- Role playingTrainees pretend to perform
- Ikhlaskan demi sesuatu yang baik
- hubungan jarak jauh tidak akan bertahan
- 7.5 Factors Influencing Enzyme Reactions
- Diam diamlah
- Earthquakesthe most deadly natural hazar
- Kecantikanmu aku jadi naksir
- Ikhlas demi sesuatu yang baik
- Executive coachingOne-to-one training se
- 7.5 Factors Influencing Enzyme Reactions
- Manusia tidak ada yang sempurna..hidup a
- Earthquakesthe most deadly natural hazar
- Business gamesUsed to develop problem-so
- Lifelong learning approachCareer develop
- i hope you know but i always try to be a
- 7.5.1.1 Multiple Substrate ReactionsMost
- The effect of a competitive inhibitor de
- long distance relationship would not las
- hati hati aku berdoa sukses buat kamu
- 7.5.1.1 Multiple Substrate ReactionsMost
- The effect of a competitive inhibitor de
