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Biomolecules Cbse Pyq

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104 views10 pages

Biomolecules Cbse Pyq

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legendgaming1181
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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CHAPTER

14
Biomolecules

14.1 Carbohydrates 14.4 Vitamins


14.2 Proteins 14.5 Nucleic Acids
14.3 Enzymes

To,picwise Analysis of last 10 Years' CBSE Board Questions (2020-2011)

24 -------------- ______________________ ----------------------------------------------------- ■ VSA


0 SA
22 -------------- ~LA I
20 ffl LA II
T IS --- ---------- ----- - - - - ---------------------------------------------------------
"'
§ 16 - ----· ------------------------------------------------------------------------ - ----

·g.,::, 14 ---------· --------------·------------------------------------- ------------------------


::!:' 12 --------- --·----------------------------------------------- --- ---- --- - ---------
"'.,... 10
.0
a::, 8
z -----------
6 ·----------
4 ---------
2
0
1-U 14.2 14.3 14.4 14.5
Topic__.

►► Maximum total weightage is of Carbohydrates. ►► Maximum SA and LA I type questions were


asked from Carbohydrates and Proteins
►► Maximum VSA type questions were asked from
respectively.
Carbohydrates.

- - - - - - - ( QUICK RECAP ) ~ -- - - - --

CARBOHYDRATES
0 General formula: Cx(H 2O)y
0 Sugars or Saccharides: ·n1eyare optically active polyhydroxy aldebydes or ketones.
C) Classification :
Carbohydrates are classified as either reducing or non-reducing sugars :
~ Reducing sugars :
- Free aldehydic or ketonic group.
- Reduce Fehling's solution and Tollens' reagent
- e.g., maltose and lactose.

4 Non-reducing sugars:
- Do not have free aldehydicor ketonic group.
- Do not reduce Fehling's solution and Toll ens' reagent
- e.g.• Sucrose.
► On the basis of their behaviour towards hydrolysis :
Carbohydrates

'dJ
Monosaccharidcs Oligosaccharides Polysaccharides

Cannot be hydrolysed further. Yield large number of


Yield r arides
(CH20\.where. 11 =3-7 on hy, re - monosaccharides on hydrolysis.
e.g.. glucose, fructose, ribose, etc. (C6H I( 2- 10 (C6H 100 5) 11 ,where,11 = 100-3000
e.g., SIi, C. e.g.. starch, cellulose, etc.
C) Monosaccbaridlcs :
► Glucose (C6H 120 6) : An aldohexose as iL contains six carbon atoms and aldehydic group.
Structure : CHO

H~ti;
: CH20H :
·- ................ -·
Fischer plllJc<:tJOn of
D-(+).Clucosc
6
C H OH
H

H
"
r.t•D-(+)·Glucopyrruiose ji--D-{+)-Clucupyranose
HJl\llr1h ,tructure-,:
(Anom~rs)
Preparation :

C12 H220 11 + H 20 ~ C6 H 120 6 + C6 1I 120 6 (Laboratory mctl,oti)


Sucro,,c GI ucose Fructu54!

Hi/.:\ )
(C6H 100 5),, + 111-120 11C6 H1206 (Commercial metliod)
Starch urCellul<l><!
3~3 K, 2-1 atm Cluco'<!
Gluco11e w as a'i Si
gn ed o pe n c 11a m stru c tu re on
th e ba sis of follo wi
ng e, ·id en ce s:
C H1 +C H :! 1i C H ~ 111 i.
l '
(~" ca rbo n a tom ,. IO ~B rrw ate r
CO OH
,,..1 L~,a.ne
lm kr o m a stn ,g ht ar.- .
,
I
m.am) (indicat<-,, .i\d clw d (rHO H) .i
IC
i;r ou p)
CH20 H
C H = N OH C.lururu, .i<1d
I CHO
(CJ lO H ),. - ~ H ~O H I CH O
~

(C H O H ) 5< 0 13CO )i0 tznCh


I .
C H 20 H
Gl uC \~ {'lx1mt..
(co nh rm s the pre :.c
n-x of a
c.u bo ny l gr uu p)
I
C H20H
4
(« mh rrn , the pr,:-·""'" nf
fiw -OH gn ,up ,,)
.
(1I HOCOCH )i 3
LluC<lM' C H 0C O CH
2 3
Gl uc ose ? ft '~ "'
CH_,,,,.C\I
I '0 1 1 . CO O H
IIC N JU..:OJ"O>-id.lhon
(C H O I 1) ' . I
4 lm J,c at, es th. , r ~ -,,, (C HOH )
I (n mh rrn , th. , pn :-- nt. , 4
·nn • of a
CH:!OH c•rb<>nyl gro up ) pn rna ry alcuho1lic (-
O H) I
gn,up) COOH
Gl uc os e cy an oh yd Cl ua ric o1ciJ "r
nn
5.K ,h. im a~1J
C hem.icnl re ac tion
s: or Gl~,·anc ..a d
R ed uc tio n:
C H ~O H CH O
I - I
(CH O H)-1 . 'la -H g l'y r,J m. : .
.
(CH O CO CH ,) ,
I
I ' .~
C H201 1 G l20C O C H
3
C).<;orb1tol ,. Ou o,t u I Ou t to GluCOSC' p(!"'taan-tal
- -CIIO ~
I G lu co se 11 -O H. , (a m1 '1U re "' ,..
and jl-f<> m<I
O xi da tio n: gr ou p ~ up
H C H30...._
C u 0 - + G lu co ni c ~ f,· hh n1 fs 'c -O CH 3 H
010 c✓--~
2
' -.o luh on
I
b
o-1,01-1
Red pp t. ac id I . I
(CH C l).i ~SPC4 d~ HO ,:a , (<fHOH ), 0 + (~ H O H h
follM\S I
2A~.!. + G lu co ni c . re. igc nt CH - - - '
Si hc r ac id
- C H2CI
Pc nr ac hl, ,~ lua )', I
CH - - - '
I
nu rro r
(G luc os c pcntachlon
t C H20H C H :P H
► Fructose (C H O
d,• ) o-O-l\lelh\'lgluco,-1J, l}- 0.\ tet h, lglun>s
ide
) : A ke to he xo se as it co
6 11 6 nt ai ns six ca rb on at
oms an d a keto01c gr
Structure: oup.
t.H ~O I l
2I -
C=0
HO
4 ~ll
H OH
H ,; 011
6
C ll20 H
D (· ) I ructo,,,•
b
I
H O H2 ; ~ 0
:CH f> H
H 110
11 OH
4 3

OH H OH II
ot• D-{ -)-1 ru ct, ,fu
ran o,
P-D·(- Fructolur...,
.,..,
(H~\\"Orth St n1ctu rn
)
C) Properties : ► The products formed by the linking of amino
► In aqueous solution, the carboxylic group can acids by peptide linkage are known as peptides.
lose a proton and amino group can accept a ► Peptides are further divided into di, lri, tetra
proton giving rise to a dipolar ion known as depending upon the number of amino acids
z witter io11. 'This is neutral but contains both combined.
positive and negative charges. ► Oligopeptide : It contains anywhere between
0 0 2- 10 amino acids.
II II
R-CIJ-C-OH R-CH-C-0 ► Polypeptides : Structures with more than
I I
:NH2 Nrr3

N~"c::i'{·:;:~·::)1w::~::::H
+
U-dminu ,u;ld Zw1tter mn

► Since these form salts with acids as well as H


2
with bases, their chemical reactions are I I I
R R' II R"
similar to primary amines and carboxylic acids.
0 o.w 0
1'
N-tcrminal
t
C-termlnol
R-CH-Cq < R-CH-Cq .ut\l.no .1.dd amino ..icid
, "o- 11• , "o- where, R, R', R" may be same or different
NI-r2 +NH3
► A polypeptide with more than hundred
(in alkaline solution) (Neutral form) amino acid residues, having molecular mass
n• ij'o higher than L0,000 u is called a protein.
-<- -> R-CII-C
OW I "OH C) Classification of proteins : On the basis of
1
NH3 molecular structure, proteins arc classified as:
(in acidic solut ion) Fibrous proteins ]
► Isoeleclrk p o int: The pH a l which dipolar
ln fibrous proteins, polypeptide chains are parallel
ion (zwiller ion) exists as neulraJ ion, i.e., r3
and are held together by hydrogen and disulphide
+ve and - ve charge is equal and it does bonds. These are insoluble in water,e.g., keratin and
not migrate to either electrode, is called myosin.
isoelectric point. lhe amino acids have least
solubility in water at isoelectric point which Globular proteins I
helps in their separation. Globular proteins result when the polypeptide
Except glycine, all other naturally occurring y
► chains coil around to give three dimensional
a -amino acids arc optically active because spherical shape. These are soluble in water, e.g.,
they contain chiral, asymmetric carbon atom. insulin and albumins.
► They exist in both D- and L-forms. Most C) Structure :
naturally occurring a-amino acids have Primary structure : lt refers to lhe number

L-conliguralion. and linear sequence of amino acids held
COOH
al togelher b)' peptide bonds.
11,N-C-11 11 0 H R' f I OIi
- I I II ""-c/ I
R
L-A mino acid
/N....__
C
,.,..c, N / . .__C /N....__ C /C"-,
C) Peptides and their classificatio n : H/ ""-R ~ g H/ 'R''
► Peptide bond : The bond formed between Primary ,tructurc
two amino acids by the elimination of a water ► Secondary structure: It is due to folding or
molecule is called a peptide li11knge or bond. coiling of the peptide chain. lt is mainly of
,...,.....- ---,...,., -Hp two types:
-C-jOH + HrN-
11 ..___ _ I
> -C-N-
11 I - ~-helix : These coils are stabilized by
0 H '-0 H___, hydrogen bonds between carbonyl oxygen
Carboxyl group Amino group of first amino acid to amide nitrogen of
of one of other Peptide bond
ruruno acid amino acid fourth amino acid.
- f3-pleated sh eet structure : f3-pleated EN'.ZYMES
sheet structure ls formed when hydrogen C) ·n,e enzymes are biocatalysts produced
bonds are formed between the carbonyl by living cells which catalyse biochemical
oxygens and amide hydrogens of two or reactions in living organisms. Chemically,
more adjacent polypeptide chains. The enzymes are naturally occurring simple or
bonding in f:3-pleated sheet structure is conjugated proteins. Some enzymes may be
intermolecular H-bonding. The structure non-proteins also.
is nol planar bul is slightly pleated. Silk HORMONES
nbroin is rich in f3-pleated sheets. C) Hormones : They are the molecules that act
as interceiluJar messengers and are poured

i
a-heh~
r g., myosm {nucleus),
keratin (hair) etc.
lntlivldu•I
polypeptide
chain.,

l!-pl~•IL'<l ~h l'l:l
e.g, silk p l'\ltl'in (f1hroin)
C)



directly in the blood stream by endocrine glands.
Types of hormones :
Steroids : Estrogens and androgens
Polypeptides: Insulin and endorphins
Amino acid derivatives : Epinephrine and
norepinephrine.
► Tertiary structure It represents overall VITAMINS
folding of the polypeptide chains i.e., further
Vitamins: These are complex organic
folding of the secondary structure and the
molecules which cannot be produced by Lhe
bonds re!tponsible for such interaction are body and must be supplied in small amounts in
hydrophobic interactions, hydrogen bonds, diet to carry out essential metabolic reactions
ionic interactions, van der Waals' fo rces and which are required for nonnal growth and
disulphide bonds. maintenance of Lhe body.
► Quaternary structure : The spatial arrange- Classification :
ment of the subunits (two or more polypeptide Water soh1ble vitamins : Soluble in water.
chains) with respect to each other. Must be supplied regularly in diet as they are
regularlyexcreted in urine (except vitamin B11) ,
C) Dcnaturation of proteins : e.g., Vitamin- 8 1, B2, 86, B12 and C.
► When a protein in ils native form, is Fat soluble vitamins : Soluble in fat and oils.
subjected to physical changes like change in Stored in liver and adipose tissues, e.g.,
temperatLtre or chemical changes like change Vitamin - A, D, E and K.
in pH, the hydrogen bonds arc disturbed.
Due to this, globules unfold and helix gets C) Deficiency of more rhan one vitamin in the
body causes avitaminosis while excess intake of
uncoiled and protein loses its biological
vitamins (A and D) maycausehypen1ilnmi11oses.
activity. This is called de11nturation ofprotein.
NUCLEIC ACIDS
► The denaturation causes change in secondary
and tertiary structures but primary structure Nucleic acids are the polymers of nucleotides
remains intact, e.g., coagulation of egg while present in nucleus of all living cells and play
on boiling, curdling of milk, formation of an imporlant role in lransmission of the
hereditary characteristics and biosynthesis
cheese, when an acid is added to milk.
of proteins.
Nudeollde

Pentose sugar Ni trogcnou~ ba~c Phosphate group (POf)


Deoxynbose
Ribose
i
-o - P- 0-
♦ ♦ 1
Pyrimidine Purine 0
Uracil (U) Adenine (A)
Thyminc (T) Guanine (G)
C}1osme (C)
C) Types of nucleic acids : two H-bonds (A= T) and guanine (G) pairs
Nud,ic acids with cytosine (C) through three H-bonds
=
(G C). In case of RNA, adenine (A) pairs
Deoxyribonucleic acid Ribonucleic acid
=
with uracil (U), (A U).
(DNA) (RNA) C) Replication : It is the process by which a
single DNA molecule produces two identical
copies of itself.
Messenger Ribosomal Transfer C) Protein synlhesis : It occurs in two steps:
RNA(m-RNA) RNA(r-RNA) RNA(t-RNA)
► Transcription : IL is the process of synthesis
C) Cbargaff's rule: Amount of purine bases is ofRNA.
always equal to that of pyrimidine bases. ► Translation : The synthesis of proteins occur
Purine base of one strand of DNA molecule in the cytoplasm of the cell. The 111-RNA
pairs with pyrimidine base ofthe other strand. directs protein synthesis with Lhe help of
Adenine (A) pairs with thymine (T) through r-RNA and t-RNA.

BB << < > >> ~ ~ X


14.1 Carbohydrates 12. Write the product obtained when D-glucose
reac ts withH2N-OH. (Al 2015)
••4H (1 mark) 13. Which one of the following is a
1. Name the clisaccharide which on hydrolysis monosaccharide :
gives two molecules of glucose. starch, maltose, fructose, cellulose
(One word, 2020) (Foreign 2015)
2. Write the name of linkage joining two 14. Whkh of the two components of starch is
monosaccharides. (One word, 2020) water soluble? (Delhi 2014)
3. a-D( +) glucose and ~-D( +) glucose are 15. Write the product formed o n reaction of
(a) geometrical isomers D-glucose with Br2 water. (Del/ii 2014)
(b) enantiomers 16. Write the product formed when glucose is
(c) anomers treated with HI. (Del/,i 2014)
(d) optical isomers (2020) 17. Dcfme the following term:
4. Assertion (A) : Sucrose is a non-reducing Anomers (Al 2014, Foreign 2014)
sugar. 18. Define lbe following term:
Reason (R) : Sucrose has glycosidic linkage. Polysacch arides (Foreign 2014)
(a) Both Assertion (A) and Reason (R) 19. Deline lbe following term: Invert sugar
are correct statements, and Reason (Foreign 2014)
(R) is the correcl explanation of the
20. What is a glycosidic linkage? (Delhi 2013)
Assertion (A).
(b) Both Assertion (A) and Reason (R) 21. Name two components of starch.
are correct statements, but Reason (R} (Dell,i 2013C)
is not the correct explanation of the 22. Write a reaction which shows that all the
Assertion (A). carbon atoms in glucose are linked in a
(c) Assertion (A) is correct, but Reason (R) straight chain. (Al 2012)
is incorrect statement. 23. Stale two functions of carbohydrates.
(d) Assertion (A) is incorrect, but Reason (Al 2012C)
(R) is correct statement. {2020)
24. Explain what is meant by lbe following:
5. What is the basic structural difference Pyranose structure of glucose?
between glucose and fructose? (Del/Ji 2019) (Al, Foreign 2011)
6. Write the products obtained after hydrolysis
of lactose. (Delhi 2019)
25. Define Lhe following terms:
7. Deline the following with an example of:
(i) Oligosaccharicles
Polysaccharides (113, 2018)
(ii) Invert sugar (2020)
8. Write the product when D-glucose reacts with
26. Write the reactions showing the presence of
cone. HN03• (l/ 3, 2018, Al 2012)
following in the open structure of glucose:
9. Write the name of two monosaccharides (i) an aldehyde group
obtained on hydrolysis of lactose sugar. (ii) a primary alcohol (2020)
(Delhi 2016)
27. Enumerate the reactions of glucose which
10. \Vrite the structural difference between cannot be explained by its open chain
starch and cellulose. (Al 2016) structures. (Dell,i 2014C, Al 2011)
11. Which one of the following is a disaccharide: 28. Write any two reactions of glucose which
Starch, Maltose, Fructose, Glucose? cannot be explained by the open chain
(Delhi 2015) structure of glucose molecule. (Delhi 2012)
29. Write down the structu res and names of 39. What is the difference between fibrous
the products formed when D-glucose is protein and globular protein?
treated with (i) Hydroxylamine (ii) Acetic {1/3, Al , 20liC, Delhi 2015)
anhydride. (Al 2012C} 40. Give one example each for fibrous protein
30. Write down the structures and names of and globular protein.
the products formed when D-glucose is (Al 2016, Delhi 2014, AI 2013C)
treated wilh
4 1.Amino acids show amphoteric behaviour.
(i) Bromine water
(ii) Hydrogen iodide (Prolonged heating). Why? (Al 2015)
(Al 2012C) 42. What is the diO"erence between acidic amino
31. Whal is essentially the difference between acids and basic amino acids? (Foreign 2015)
a-form and ~-form of glucose? Explain. 43. What type of linkage is responsible for the
(Delhi 2011) formation ofpro1eins? (Delhi, Foreign 201 11)
44. Define the following term :
■ ti■ (3 m_a_r_ks~)~ - - -- -
Essential amino acids (Al 2014)
32. Give the plausible explanation for the
following: 45. Define the following term:
(a) Glucose doesn't give 2,4-DNP test. Denaturation of proteins (Foreign 2014)
(b) The two strands in DNA are not 46. Define the following term :
identical but are complementary. Amino acids (Foreign 2014)
(c) Starch and cellulose both contain
47. Define a 'peptide linkage'.
glucose unit as monomer, >'el they are
slruclurally different. (2020) (Al 2014C, 2011, Foreign 2011)

33. Write chemical reactions to show that open 48. Where does the waler present i11 the egg go
structure of D-glucose contains the following: after boiling the egg? (Delhi 2012C)
(i) Straight chain •-~:!r.1:.■
-■ (2 marks)
(ii) Five alcohol groups
49. Define the following with an example of
(iii) Aldehyde as carbonyl group. (Delhi 2019)
each:
34. What happens when D-glucose is treated (i) Denatured protein
with the following reagents? (ii) Essential amino acids (2/3, 2018)
(a) Br2 waler
(b) IICN 50. (a) Amino acids show amphoteric behaviour.
(c) (CH3C0)20 (Al 2019) Why?
35. Define the following terms : (b) Write one difference between a-helix and
(i) Glycosidic linkage f3-pleated struclures of proteins.
(ii) Invert sugar (2/3, 2018)
(iii) Oligosaccharides (Al 201 1I} 51. Describe what you understand by primary
36. What is essentially the difference between structure and secondary structure of
a-glucose and ~-glucose? \Vhat is meant by proteins? (Delhi 2011 , Foreign 2011)
pyranose structure of glucose? (Al 2012) 52. Explain what is meant by a pepLide linkage.
37. Mention the structural feature characterising (Delhi 2011)
reducing sugar. (Dell,i 201 JC)
Mf-1• (3 marks)
14.2 Proteins 53. Dilforentiatc between the following :
U1Zli (1 mark) (i) Amylose and Amylopectin
38. Peptide linkage is present in (ii) Peptide linkage and Glycosidic linkage
(a) carbohydrates (b) vitan1ins (iii) Fibrous proteins and Globular proteins.
(c) protein (d) rubber. (2020) (Delhi 2019)
54. Define the following terms as related to 69. Name the only vitamin which can be
proteins: synthesized in our bodr Name the disease
(i) Peptide linkage caused due to the deficiency of this vitamin.
(ii) Primary structure (Delhi 2013C)
(iii) Denaturallion (Al 2015, 2014) 70. How are hormones and vitamins different in
55. What are essential and non-essential amino respect of their source and functions?
acids? Give two examples of each. (Al 2013C)
(Al 2014C, Delhi 2012C) 7 1. Name Lhe deficiency disease resulting from
56. (a) Give hvo dilTerences behveen globular lack of vitamin A in the diet (Dell,i 201 lC)
and fibrous proteins. 72. 1 he deficiency of which vitamin causes the
(b) What change occurs in the nature ofegg disease, 'pernicious anaemia'? (Al 201 JC)
protein on boiling? (Delhi 20J3C)
■ffl■ (3 marks)
14.3 Enzymes 73. How are vitamins classified? Name the
vitamin responsible for Lhe coagulation of
Ki!• (1 mark) blood. (Delhi 2015C)
57. Define Lhe following term:
Enzymes (Foreig1120 14, Al 2014 C) 14.5 Nucleic Acids
58. \Nbat is meant by biocatalysts? (Delhi 2012) Willi Cl mark)
74. What is difference between a nucleoside and
14.4 Vitamins nucleotide? (Delhi 2016, 20J4C)
Uft (1 mark) 75. What type of linkage is present in nucleic
59. Why vitamin C cannot be stored in our
acids? (Al 2016)
body? (Del/1i 2016) 76. Name of lhe base Lhal is found in nucleoLide
of RNA only. (Delhi 2014)
60. Write the name of vitamin whose deficiency
causes bone deformities in children. 77. Define the following term:
(Delhi 2015) Nucleoside (Foregin 2014)
61. Write the name of the vitamin whose 78. Mention one imporlanl function of nucleic
deficiency causes bleeding of gums. acids in our bod}'· (Al 2013C)
(Foreign 2015) •-~:f";■
- (2 marks)
62. Deficiency of which vitamin causes nlght- 79. Write the st ructural and functional difference
bliodness? (Delhi 2014) between DNA and RNA. (Delhi 2013C)
63. Deficiency of which vitamin causes rickets? 80. Write the main structural difference between
(Delhi 2014) DNA and RNA. Of the two bases, thymine
64. Deficiency of which vitamin causes scurvy? and uracil, which one is present in DNA?
(Delhi 2014) (Delhi 2012)
65. Define the following term : 81. Name the bases present in RNA. Which one
Vitamins (floregi11 2014) of these is not present in DNA? (Delhi 2011)
82. Write the main structural difference between
66. Why are vitamin A and vitamin C essential
DNA and RNA. Of the four bases, name
for us? (Delhi 2014C)
those which are common lo both DNA and
67. Name the deficiency diseases resulting from RNA. (Al 2011)
lack of vitamins A and E in the diet
(Delhi 2013C) ■tJ■ (3 marks)
68. Name one of the water soluble vitamin which 83. Whal are the different types of RNA found
is powerful antioxidant. Give its one natural in cells of organisms? State the functions of
source. (Delhi 20JJC, Al 2012C) each type. (Delhi 2012C)
Detailed Sol r
1.
l.
M al to se
G ly co si di c lm ka ge glucose um ts. lo sta
V
. rc h, there is a-D-gl
hn ka ge . Bo th th e co ycosidic
3. (c ) :T he pa ir m po ne nl s of starch-
of sl er eo is om er s w amylose
on ly in th e co nf ig ur hi ch di ffe r an d am yl op ec lin ar
at io n of th e hy dr ox e polymer of o.-D-
y\ gr ou p at O n tb e ot he r ha nd , ce g.lucosc.
C , ar e ca lle d an om er llulose i!> a linear po
s. of 13- D-glucose in lymer
which C 1 of on e
un il is co nn ec le d gluco-..:
H-~CEl lo C 1 of th e ot he r
H H O- ~ ~ (3-D-glycosidic lin ka th rough
1-i ge.
01 £ 11. M aho se 1s a di
H ~OH
0 \ saccharide as it cons
o.-D-glucose un ib . ists of two
1 1 0 -~- - H
1 0
H 0 -=3-1- -- ll
12. D- G \u co~e re
ac ts with H 21' :- 0H
H -- -+ -- O H
H -- 4 g\uco<.e ox im e. lo give
OH
CHO
H -. .. 1 !- -\ -- -- C tt = N -O H
~ H -- "' "+ -- -- ~ I I
(C llO H ) + N H 20H ~
CH 0H 1 (C HO H)
1,
2
6
CH20H I I 4
a- D -( +) G lu co se C H 20H
~ D (+ ) Glucose
CH 20H
4. (a) : Su cr os e is di 13 . Fr uc to se is a
sa cc ha nd e an d 1ls monol>accharide be
tw o ca nn ot be hydrolys cause 1t
m on os ac ch ar id cs ed to simpler po:y
ar e he ld to ge th er by hydroxy
lin ka ge . Si nc e th a gl yc os id1c a\ de hy de s or ke lo ne
e re du ci ng gr ou ps s.
an d fr uc to se ar e of gl uc os e 14 . A m y\ os e is wa
in vo lv ed in gl yc os ter soluble an d am )lo
id ic bo nd pe cl in is
fo rm at io n, th er ef or in so lu bl e m "a te r.
e, su cr os e is a no
n- re du ci ng 15 . D -G \u co se ge b
su ga r. ou di se d to carboxyl
(g \u co ni c ac id ) on re ic acid
s. G lu co se co nt ai ru . an ac tio n with br om in e
waler.
al de hy di c gr ou p w CHO
fr uc to se co nt ai ns a hile CO O H
ke to ru c gr ou p. I &r ! .wa1cr
6. La ct os e on hy dr (C HOH)-1 'ClH O H )
ol ys is gi ve s 13-D-g ➔ , ~
\ucose an d I I
!3 -D -g ala ct os e. CH 0 H
2 CH 20 H
7. C ar bo hy dr at es D-GILl~O..C Glucoruc ac d
w hi ch yi el d a la rg 16. O n pr ol on ge
of m on os ac ch ar id e nu m be r d he at in g with HI .
e un its on hy dr ol ys D-gluco-.e
b ar e ca lle d fo rm s 11-hexane.
po ly sa cc ha rid es , e.g
.• ce llu lo se .
8. O n ox id at io n CHO
"; th ni tri c ac id . I
yi el ds sa cc ha ric ac
D -g \u co se (CHO H ) 4 HI . ~ ➔ CH 3- (CH 2)-1 -CH3
id . I n-H cu nc
CHO COOH CH 20 H
I cone. HNO, ) I D-Glucosc
(C H O H )1 (C H O H ) l 7. Rejer to answer
I I 3.
C H !O H COOH 18 . Refer to 1111swer 7.
D-gluco~ D S3Cchanc ao d . la r m ix tu re of d
1 9· A n equ1rno glucose an
9. Refer to a11swer 6. . d b bydroly~i!>
fru ct os e, ob ta in .
e Y of sucrose m
\ di ff er en ce bct w n pr es en ce of an ac1.d .
10 . Th e ba si c st ee . or
th e en l)' m e in vertase ·,~
ru ct ur a . be tw ee n th e ca lle d in \'e rt sugar.
\ ·an d ce llu lo se is of lin ka ge
st ar e,

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