Vongai C. Mlambo Friday 4th March 2013 Biology Internal Assessment The ydrolysis !

" #$crose By In%ertase

Table 11 #ho&ing Time Ta'en For #$crose(In%ertase Mi)t$res *)tracted At +i""erent Times To +ecolo$rise ,Mn! 4
Time #ol$tion &as e)tracted -min.

Time Ta'en For #ol$tion To +ecolo$rise ,Mn!4 -seconds. /3s

1 3 5 10 15 20 25 30 35

1 031 331 202 142 120 130 112 114 114

2 141 334 302 211 140 121 131 133 112

3 023 303 223 211 142 132 132 130 132

4 101 302 220 222 142 120 131 110 114

5 121 323 221 202 120 130 111 123 113

6 330 332 323 201 144 120 110 120 104

A66arat$s 0ml #yringe 100ml Meas$ring Cylinder 10ml #yringe 2.0ml #yringe

Table 2 #ho&ing 5ncertainties !" A66arat$s 5sed 7eagent 5ncertainty-/cm3.

Vol$me Meas$red-cm3. 0 100 10 2.0

#$l6h$ric Acid #$crose #ol$tion #$crose(In%ertase Mi)t$re 8otassi$m 8ermanaganate

0.2 1 0.0 0.20

The data recorded "or trials 3 to 1 &as obtained "rom the "ollo&ing 6eo6le9 annah :)$malo; <ise Arge; Agathe Cha6elle; =ae >oo,im; Ambar Ahmed; =esca Cheng$la ; A$g$stine and ,itty Tric's.

Table 3 #ho&ing ?$alitati%e +ata !bser%ed +$ring The *)6eriment

!bser%ation :o.

!bser%ation
#$crose(In%ertase sol$tions e)tracted a"ter a longer 6eriod o" time e.g. 10 min$tes got lighter in colo$r than those e)tracted at an earlier stage; e.g. 1min In trial 1 and 2 at 10 min and trial 2 at 30 min; a 6in' ring &as seen at the to6 o" the sol$tion

1 2

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Table 4 #ho&ing Mean And #tandard +e%iation !" 7a& +ata

Time sol$tion &as e)tracted -min. Time Ta'en-s. Mean #tandard +e%iation *stimated @l$cose Concentration -A. Mean #tandard +e%iation

1 3 0 10 10 20 20 30 30

131 313 240 214 140 133 130 113 102

21 20 23 20 4 4 1 22 24

Table 0 #ho&ing Concentration !" #ol$tion 5sing Mean Time Ta'en To +ecolo$rise ,Mn!4

Time -seconds.

@l$cose Concentration

131 313 240 214 140 133 130 113 102

1.0 2.2 2.1 3.3 3.3 4.0 4.3 4.0 4.1

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The data sho&s that the rate at &hich in%ertase brea's do&n s$crose is initially high b$t then decreases as time increases. This trend is sho&n by the gra6h &hich de6icts an $6&ard c$r%e that is stee6 initially b$t 6latea$s at the end o" the c$r%e. The s$crose(in%ertase mi)t$re that &as reacting "or a longer time contained a higher concentration o" gl$cose. o&e%er; the di""erence bet&een the gl$cose concentration di""ers to a greater e)tent &ith the sol$tions e)tracted bet&een 0 B 10 min$tes than those e)tracted bet&een 20 B 30 min$tes. This is re"lected by the 6ercentage change in gl$cose concentration that can be calc$lated "rom the in"ormation in Table 0. The di""erence in concentration o" s$crose(in%ertase mi)t$res that too' longer times to decolo$rise the 6ermanganate is m$ch smaller than those that too' the least time. For e)am6le 4.0A and 4.1A too' the shortest times to decolo$rise and the 6ercent change is 0.1A &hich sho&s that %ery little gl$cose &as 6rod$ced &ithin that inter%al; b$t "or 1.0A and 2.2A &hich too' the longest times to decolo$rise the 6ermanganate the 6ercent change is 0.3A there"ore a greater amo$nt o" gl$cose &as 6rod$ced &ithin that inter%al than the "irst. This s$ggests that the rate o" s$crose hydrolysis is greater initially res$lting in greater di""erences bet&een the three initial gl$cose concentrationsC As the reaction contin$es; the rate slo&s do&n th$s the di""erences bet&een gl$cose concentrations become less and less as the gra6h begins to 6latea$ indicating that less and less gl$cose is being 6rod$ced "rom the hydrolysis o" s$crose.

This trend can be e)6lained biologically &ith the $se o" in"ormation obtained "rom &&&.amrita.%lab.co.inDEs$bF3GbrchF14GsimF.1040GcntF1 accessed on 14D03D14. Initially the amo$nt o" s$bstrate; s$crose; is high. The s$bstrate molec$les th$s ha%e a greater 6robability o" colliding into the acti%e site o" an enHyme and binding to it in order "or the catalyHed reaction to ta'e 6laceC there"ore; initially; the rate o" s$crose hydrolysis by in%ertase is high. As the in%ertase contin$es to hydrolyse the s$crose; less and less s$bstrate molec$les are 6resent. There are less s$bstrate collisions &ith the acti%e sites o" in%ertase so it bind to the acti%e site less and conseI$ently the rate o" s$crose hydrolysis declines.

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