6
HWAHAK KONGHAK Vol. 38, No. 3, June, 2000, pp. 434-439 (Journal of the Korean Institute of Chemical Engineers) 434 * * (2000 2 18 , 2000 3 14 ) Mid-Scale Deinking Process for Office Waste Paper Recycling using Cellulase Sang-Mok Lee, Keun-Garp Ryu* and Yoon-Mo Koo Department of Biological Engineering, Inha University, Inchon 402-751, Korea *Department of Chemical Engineering, Ulsan University, Ulsan 680-749, Korea (Received 18 February 2000; accepted 14 March 2000) Trichoderma reesei Rut C-30 crude cellulase papain cellulase . Novozym 342 , . crude cellulase CMCase activity 3 units/g Oven Dry Paper (brightness) (freeness) . . 3 units , 2 units . Papain Novozym 342 , , . Trichoderma reesei RUT C-30 crude cellulase papain endo exo (Novozym 342) , . Abstract - Enzymatic deinking of office-waste paper was studied using crude cellulase and papain-hydrolyzed cellulase from Trichoderma reesei Rut C-30 in small-scale and mid-scale. The results were compared with deinkings using commercial enzyme(Novozym 342) and conventional chemical methods. Maximum brightness and freeness were obtained at 3 units/g Oven Dry Paper(ODP) of CMCase activity using crude cellulase in mid-scale deinking experiments. The deinked pulp had higher physical strength and brightness, and lower freeness and yield than the pulp deinked in small scale. In small scale deink- ing, maximum brightness and freeness were obtained at 2 unit/gODP. Deinking by papain-hydrolyzed cellulase showed similar results with those by Novozym 342. It was better in brightness and freeness, but showed lower physical strength and yield, than the conventional deinking by sodium hydroxide. The ratio of endo-1,4-glucanase and exo-1,4-glucanase components in papain- hydrolyzed cellulase from Trichoderma reesei Rut C-30 was similar to that of commercial enzyme, Novozym 342, implicating a successful application as a deinking enzyme. Key words: Cellulase, Enzymatic Deinking, Papain, Brightness, Freeness, Physical Strength E-mail: [email protected] 1. . . . , , , , pitch control , cellulase, hemicellulase, xylanase, lipase, peroxidase [1, 2]. , . , , ,

Mid-Scale Deinking Process for Office Waste Paper ... · Sang-Mok Lee, Keun-Garp Ryu* and Yoon-Mo Koo† Department of Biological Engineering, Inha University, Inchon 402-751, Korea

  • Upload
    others

  • View
    2

  • Download
    0

Embed Size (px)

Citation preview

Page 1: Mid-Scale Deinking Process for Office Waste Paper ... · Sang-Mok Lee, Keun-Garp Ryu* and Yoon-Mo Koo† Department of Biological Engineering, Inha University, Inchon 402-751, Korea

HWAHAK KONGHAK Vol. 38, No. 3, June, 2000, pp. 434-439(Journal of the Korean Institute of Chemical Engineers)

�������� � �� ����� ����

�������*��†

����� ���� ����*���� ���� �����

(2000 2� 18� ��, 2000 3� 14� ��)

Mid-Scale Deinking Process for Office Waste Paper Recycling using Cellulase

Sang-Mok Lee, Keun-Garp Ryu* and Yoon-Mo Koo†

Department of Biological Engineering, Inha University, Inchon 402-751, Korea*Department of Chemical Engineering, Ulsan University, Ulsan 680-749, Korea

(Received 18 February 2000; accepted 14 March 2000)

� �

Trichoderma reesei Rut C-30�� ��� crude cellulase� �� �� ����� ��� papain�� �� ��

��� cellulase� ���� � !"� #$% &'()* �+�,. � &'()� -.� /0� &'��� Novozym

342� ���1 ��2 &'()., �3�� 4��1 56 782 &'(). 9:�,. #$% &'()�� crude

cellulase ;<� => &'�?@ CMCase activity AB 3 units/g Oven Dry Paper�� �C<(brightness)� ��<(freeness)

� DEF* G,. �$%� 9� HI2 J<� �C<� KL�M ��<� �?@ NL. #$%� OP 3 units��

�C<� ��<�� D2� QR, �$%� OP1 2 units� OP� D2S* G,. Papain TI� ��� �� &'@

Novozym 342� 9U� -.� G,�, �3�� 4��1 AV� &'()� 9��1 �C<� ��<1 P��,�

M HI2 J<��1 � NL�, �?R��< N@ -.� MWX. Y Z[�� Trichoderma reesei RUT C-30� �

� ��� crude cellulase� papain�� TI� ��� endo 3�. exo 3�� \]9?� /02�� ��^1 &'�

�(Novozym 342)� 9U�_ MW`�a, �1 Ob3c1 &'� ����� �d3* G�ef.

Abstract − Enzymatic deinking of office-waste paper was studied using crude cellulase and papain-hydrolyzed cellulase

from Trichoderma reesei Rut C-30 in small-scale and mid-scale. The results were compared with deinkings using commercial

enzyme(Novozym 342) and conventional chemical methods. Maximum brightness and freeness were obtained at 3 units/g

Oven Dry Paper(ODP) of CMCase activity using crude cellulase in mid-scale deinking experiments. The deinked pulp had

higher physical strength and brightness, and lower freeness and yield than the pulp deinked in small scale. In small scale deink-ing, maximum brightness and freeness were obtained at 2 unit/gODP. Deinking by papain-hydrolyzed cellulase showed similar

results with those by Novozym 342. It was better in brightness and freeness, but showed lower physical strength and yield, than

the conventional deinking by sodium hydroxide. The ratio of endo-1,4-glucanase and exo-1,4-glucanase components in papain-

hydrolyzed cellulase from Trichoderma reesei Rut C-30 was similar to that of commercial enzyme, Novozym 342, implicating

a successful application as a deinking enzyme.

Key words: Cellulase, Enzymatic Deinking, Papain, Brightness, Freeness, Physical Strength

†E-mail: [email protected]

1. � �

��� ��� �� � � � � ��� ������ �

� ��. ��� � �� ! "� #$� %& '(�� ��

)*+� ,-!.� /0� � � 12+� 345��. 67� 34

58 9� #$� 7$ :;� � <=� ��)*+ >�8? �@

A� B�8? �CD7� ��. EF G 7:H8? 1I� �5J

�@ �K=LM 40� #$� NOP� �QR, 1I� !SQT�

EF� UV, 673WX� YZ, [\] , pitch control _� ��,

`5P� 1I� cellulase, hemicellulase, xylanase, lipase, peroxidase_

� <�P� ��[1, 2]. ��� 1I� !SQT � A aL bNB8

?� 1I� cH+ �5� <�P� �QR, de ��)*+� !.

/0� fgh� 9iP� �� EF G 7:H8? 1I� �5J

jk lDm nQT `o&�. pq rD, `s!!� `5t�T ��

�u67� vJ �w� t� � �QR, ��� `s5 �u67�

�^ G x�� 5� �, sy<�z v{� |#EFT }P~!

434

Page 2: Mid-Scale Deinking Process for Office Waste Paper ... · Sang-Mok Lee, Keun-Garp Ryu* and Yoon-Mo Koo† Department of Biological Engineering, Inha University, Inchon 402-751, Korea

�������� � �� ����� ���� 435

�8 3W �8z v{� 3WEF� �� � ��� ��� ��.

�8 `s5 �u67� 3W ��8 �� #$� 40e �CD7�

�Q�, �c& ��!.� <u� ��X �J �� �5 A ���

U�8 ����� ��X�� toner� `5QT � A �hI��

%T �5 � !�� YZ��QT� ��� 12+� ^� 5�

7 �QR, ��� � �� ! "�? �u67� YZ,-8 1

I� `5 � #$��� <�P� ��[3-5]. �r <�8 � �

YZ,-X 1I� `5QT �� � �� ��J 3WEF� �z�

V�z� !�� �hI�� �5 � YZ��8 ��? �� ��

n��[3]. de 1I8 �� YZ��J !�� �hI�� `5 �

YZ��� �� 3WEF� �� �c� �� ! "� UV�

�� `5QT �� �{�� �I1�� V�z t�� !9� �

��[7].

67� YZ8 `5P� 1IT %T cellulase G xylanase� <�

P� �QR[1, 2], de cellulase8 �� #$� 40e NOP� ��.

Cellulase� A� bacteria G ����8? W:P� �QR, soft rot

fungus� a�� Trichoderma sp.8? W:P� cellulase� 4h� �

J nQT <�P� ��. Cellulase� a�+QT, cellulose chain�

s "+QT ��x� A cellobiose� glucose� Wh � endo-β-

1,4-glucanase(CMCase), cellulose chain� �� h ¡¢!8  5 A

cellobiose� Wh � exo-β-1,4-glucanase(Avicelase), \[� cellobiose�

x� A glucose� Wh � β-glucosidase(Cellobiase)T x� � �

�[9, 10]. Jeffries _[3]J cellulase8 �� YZ1�� £¤I ��x

�X £¤I U�8 � ¥ ¦�PD �� �� ��� ^P� peeling

effectT §¨ �, cellulase� £¤I� U�8 ¦� ! �8 ^

& �� ��� 3L�� �� A L¤� G ©ª�8 �� ����

� «¬� 5� ¥ ��� <� � ��. \��, Trichoderma viride8

? x[� endo-β-1,4-glucanase� exo-β-1,4-glucanase� `5� �7

YZX endo-β-1,4-glucanase� exo-β-1,4-glucanase� synergism8 �

� ��x� 1�� <� � ��[11]. 673W,-8 `5 � ��

cellulaserJ }1I ­®T PD �QR, exoglucanase� endogluca-

nase �� synergism 1�8 ��? �-­ cellulose� EF� x�

P� nQT ¯°± ��. ²�? cellulase8 �� EF� ³c� ´

��? YZ� 1�� ��! "�?� EF cellulase� ¡¢8  5

A cellobiose� W: � exoglucanase� µ� fgh� ��. Tri-

choderma reesei� W:� exoglucanase� $}� cellulose ¦� domain

� catalytic domainQT �CD± ��, ¢V{x�1I� a�� papain

� �r #�L"� ¶¢� � �� nQT ¯°± ��. ·� papain

8 �� ¸[& cellulase� exoglucanase� Avicel x�4hJ ´~Q�,

endoglucanase� x�4hJ �I 7 �¹�� <�P~�[11,14,15].

º #$8?�, cellulase 4h� ��� Trichoderma reesei Rut C-

308? x[� crude cellulase� papainQT ��x� A endo �2

� �� cellulase� �5 A, I»¼� '»¼8? �u67� YZ,

- G 67� ½[+ �z� V�z G A�z8 @¾� ¿�8 �

A #$ À�. ·� !�� �hI�� �5 � YZ�� G cH+

QT XÁP� �� 1I� `5 � ��� YZ dh� � À�.

2. � �

2-1. ����

º #$8 `5� cellulase� Trichoderma reesei Rut C-30� fermen-

ter(2.5L, Korea Fermenter Co.)8? «v A �J crude cellulase�

ÃÄ� �5 A -� enzyme�, ¢V{ x�1I� papain� ¸[

A endo-cellulase� �2� t�XÅ enzyme� `5 À�. Cellulase

activity >-� " A CMCase activity >-��� �5 ÀQR[16, 17],

YZ,-8 �5P� 1I� !ÆÇJ CMCase activity unit� !ÆQ

T À�. 1I� unitJ 1x ÈÉ 1µmole� � Ê(ËzÊ)� W:

� � �� 1I� vQT -� À�. CMCase activity� p9� P

� }Ì� pH 5.0� Íz 50oC? ÎÎ� 1IS� >- À�. ·�,

W:& 1I� YZ12� � ! "�? cH+QT W:P� ��

Novozym 342(Novo Nordisk Co.)� 5 À�.

2-2. ����

º #$8 `5& 7o� white ledger 3{� Ï 57(Hansol Co.)

� `5 ÀQR, Laser printer(Hewlett Packard Co.)� �5 A Ð

a ¥ v� Ï` À�. 3W,- '8? aÑ+QT 7o� U�8

��& toner� !Ò+� wÓÔQT ^ � ,-QT, �[z� ��

! "�? �[,- =8 presoaking ,-� Õ� À�. 1I YZ,

-� }Ì� Table 18 �Ö×~�. Presoaking8?� 50oC� sodium

acetate buffer(pH 5.0)8? 7o� 2XØ �Ç Ùxe +Ú%~�. Dry

oven8? Ì}& Ì}7o(Oven Dry Paper; ODP) 30 g� 0.1 M sodium

acetate buffer(pH 5.0) 5Û 1 L8 Ü+ A EFÝz(consistency)� 3%

(W/V)� PzÞ � � UÆ�[!(TAPPI standard)8 ßD pulping

À�.

PulpingX Ì}7o !ÆQT 0.2%/gODP(V/W)� Ò�4h� ß

D !Ò+ pulping8 �� ��� à[� 5� zÞ �, pulping �

Ða� Â�� �CD{ � �zÞ  & �á!(0.5 L, 3 L)8 ß�

50oC8? 1I� Õ� A 40x ÈÉ �á À�. 1I�á� ^) E

F� 0.8%(W/V)� Ýz� PzÞ âÄ� � ãäã8?  & L¤

!(flotation cell, 0.85 L, 8.5 L)8 ßD x[& toner ��� ^ À

�. W:& 1I� `5ÇJ CMCase activity� !ÆQT 1-5 unit/gODP

� PzÞ Õ� A Î `5Ç8 ²å YZ 12 G ½[+ �z�

�*� æç<¹�. Novozym 342� �5� YZX ¼è }ÌJ W:

1I� YZ,-� Èa ¥ ¤7 ÀQR, 1I `5ÇJ é`v?

8? g$ � 0.1%/gODP(V/W)QT À�. 9}ê(control) ãä�

�� ¼è }ÌJ 1I� �5 � YZ,-� }Ì� Èa ¥ ¤7

P ¢7 1I� Õ� 7 �� YZ,-� �O ÀQR, �hI��

�5 � !�� YZ,-J �hI� 1%/gODP, sodium silicate 3%/

gODP, hydrogen peroxide 1%/gODP� Õ� A YZ À�[17].

2-3. �� �

ÎÎ� ,-� ^) EF� TAPPI standard T 205 sp-958 Æ A

ëU ìÇ 100 g/m2� PzÞ �í7� } �, V�z G ½[+

Table 1. Pulping, enzyme reaction and flotation conditions in enzymatic deinking process

Process Consistency*(%) Temperature(oC) Time(min) Air flow rate(L/min)

Pulping .03 50 15 -Enzyme reaction .03 50 50 -Flotation(0.85 L) 0.8 40 05 1.5Flotation(8.5 L) 0.8 40 05 3

*Pulp concentration in buffer solution(w/v %)

HWAHAK KONGHAK Vol. 38, No. 3, June, 2000

Page 3: Mid-Scale Deinking Process for Office Waste Paper ... · Sang-Mok Lee, Keun-Garp Ryu* and Yoon-Mo Koo† Department of Biological Engineering, Inha University, Inchon 402-751, Korea

436 �����������

�z� >- À�. Blank� pulping�-� ^) EF� L¤!8? Y

Z� ^¾7 �� �í7T }& nQT À�, 9}êJ 1I Y

Z,-� Èa� YZ}Ì� ¤7 � 1I� Õ� 7 �J nQT

�í7� } À�.

2-4.��(CSF), ���(Brightness) � ��� ��(Physical streng-

th)� ��

�í7� V�z� Hunter Brightness meter(Doseki Co., Japan)�

�5 A >- À�. A�z� >-J Canadian Standard Freeness

meter(Doseki Co., Japan)� �5 A >- ÀQR, ½[+ �z� �

� î�7�(Burst Index), ��7�(Tensile Index) G ��7�(Tear

Index)� ÎÎ TAPPI standard T 403 om-91, T om-88G T om-88� �

�8 ��? ÎÎ� �z� >-� �, �í7� ìÇQT �ïD Ò

: À�.

3. �� �

3-1. Papain ��� cellulase� � � cellulase� �� ��� �

��� ��� ��

YZ,-� �OP� Íz G �I�ÍÝz _ ,-}ÌJ YZ� "

� £¤I x�1I� 4h8 � ¿�� @)�. CMCase activity�

!ÆQT � crude cellulase� 4hJ pH 5� 50oC8? p9� <

�� ��[17]. Trichoderma sp.� Wh � crude cellulase� a-�

endo, exo� ðñ�� ¤7 R, endo, exo� ðñ�8 ²�? 3WE

F� ½[+� �z� �* R YZ,-X ½[+ �z� �cX�!

" A exo-β-1,4-glucanase� 4h� µ� fg� ��. CMCase�

avicelase activity� �2T �Öò endo, exo hx�� ÃÄ8 �� -

& cellulase� �� 18.7 : 1�~QR, papainQT ¸[& cellulase�

�� 38.5 : 1�~�. i �7� endo, exo hx�� ?T �å 1I�

�ÂãäJ I»¼ L¤!(0.85 L)8? >- À�. � _[17]8 � �

½[+ �z� V�z� 7�� 1IÝz 2 units/gODP8? p9� <

óQT 2 unit/gODP8? ½[+ �z� � >- À�. YZ¸[ 1

I8 9� ½[+ �z� �Â� Fig. 18 �Ö×~�. Dialyzed cell-

ulase(Prep 2)<� endo� �2� ��! "� papain [& cellulase

(Prep 1)� j �J ½[+ �z� <�� ��. �nJ endo-β-1,4-

glucanase� ��-h L"� x�8 �� @©£¤Ç� t�� �8

²å �£¤Ç� �I� ¤z R, @©£¤� t�� ���z� t�

� ¤z ! ���. Exo-β-1,4-glucanase� % Wh½J cellobiose

T? endo-β-1,4-glucanase<� ôJ � Ê� Wh��. Papain [&

1I8 �� YZ,-8? EF� ½[+ �z t� g�J £¤c�

��-h ¿õ� �-h ¿õ� c� �ÒT §¨&�. ö, ��-h

¿õ� ��x� A @©£¤� Wh � endo-β-1,4-glucanase� d

- Ýz �c� �� @©£¤� vJ t�P� c9+QT ÷¥ ��

x�P7 �J �-h ¿õ� t�� �±�! �8 L¤X EF�

½[+ �z� �I � nQT WÎ&�. ��� ��� endo-β-1,4-

glucanase� exo-β-1,4-glucanase� +¶� }ñ� EF �z t�8 ¿�

� Æ�� �=� #$ <�� a¾��[9, 10]. i ãäê8 9� �

2� V�z, A�z� � ãä��� Table 28 �Ö×~�. A�z

� >�8?� �ø� ��� �Ö×� �Q�, �2J -� 1IT

YZ� ��� ��, V�z8?� ùJ ��� �Ö×� ��. � �

�� LcL¤X @©£¤� �¬� <� ôJ v� ����� ú±

��! �� nQT �Ä��. A!? �2�û YZ�-8? rD�

� 7o� üÇ8 9� YZ �� 7oÇ� �� �Ö×R, V�z�

Ñ�(brightness difference)� 100%� V�z� !ÆQT A LcL

¤= V�z� LcL¤ � V�z� Ñ� �Öò�. ·�, A�z�

1,000 mL� !ÆQT A 7oÛ × @©£¤� Ýz8 ²� � �

A�Û� Lý� ¡��.

3-2. �� ��!" �#$� %#$ ����� ��

V�z� ��+ >�8? YZ,- ' �� 'g� ��� � �

��þ, �� V�z� t�� �7 3WX UV� `5Ç� ´óQ

Tÿ �{��� �I 1�� !9� � �! ���. ·�, A�z

� EF G 7 :H8? ,H 5�� ��8 9� ��-z� �Ö

×! �8 ,-c8? 'g� gIT A�7� ��. ,-c8? A

�z� �I� @©£¤, ��½� �I _� +� �c� �±�R

�� EF� �z� �IX�� g�QT <�P� ��. ���

� �� ! "�? cellulase� �5� Sarkar _[13]J A�z� t�8

cellulase� !A� �, 1I� ��� `5� �XØ� 1I �áJ

�e° EF� �z� �IX�� nQT <� � ��. º ãä8?

� '»¼ YZ,-8?� p+ 1IÝz� �! "� V�z� A�

z� !ÆQT A 1-5 units/gODP� �v� 1IÝz8? YZ,-

� �O À�. ãä��8 � � 1IÝz� t��8 ²�? A�z

Fig. 1. Physical properties of deinked pulp using either papain hydro-lyzed cellulase(Prep 1) or dialyzed cellulase(Prep 2).

Table 2. Yield, freeness and brightness of deinked pulp using either pa-pain-hydrolyzed cellulase(Prep 1) or dialyzed cellulase(Prep 2)

Prep 1 Prep 2

Yield(%) 89.41 91.45Freeness(mL) 695 698Brightness difference(%) 8.4 7.8

Fig. 2. Brightness with varying enzyme concentrations.

���� �38� �3� 2000� 6�

Page 4: Mid-Scale Deinking Process for Office Waste Paper ... · Sang-Mok Lee, Keun-Garp Ryu* and Yoon-Mo Koo† Department of Biological Engineering, Inha University, Inchon 402-751, Korea

�������� � �� ����� ���� 437

� V�z� �� t� �, CMCase activity� !ÆQT� cellulase

3 unit/gODP �c8?� �Ñ �I�� Fig. 2� 38? �Ö×~�. �

�� ��� cellulase� �5 A YZ� �O À !�� #$ ��

� a¾ R[11, 17], 1I� Ýz� t��8 ²å 1I, x[& ���

�, @©£¤Ø� hydrophobic interaction� t�8 ��? LcL¤X

����� 12+QT ^P7 ! �� nQT �Ä��. '»

¼ YZ,-8? A�z� V�z� p+� �J 3 unit/gODP, ½[+

�z� 2 unit/gODP� 1IÝz8? �Ö��. I»¼8? 2 unit/gODP�

`5� � _[17]� #$ ���� Ñ�� �á!� $}� »¼, Â�

z _8 !�� nQT <��. '»¼� I»¼ L¤8 �D? V

�z� A�z� �Â� Fig. 4� 58 �Ö×~�. L¤!� $}� �

!8 �� !Ë �!� �*T �� V�z� �� I»¼� ��<�

�¥ ���. '»¼� ��, LcL¤X �! z� t�T � A !

Ë� �!� a�+QT �7� n� �Ó À�, ��� �cJ a-

� �"8? !Ë� �!� ��Þ ��@��r� ^P� 12�

��N�� #$ <�� a¾��[8]. YZ,-8? V�z� ��� �

�� <�� �2 ãä8?� I»¼� ��� �¥ �Ö��þ(Table 3),

�� 1I�á8 �� @© £¤Ç� t�� I»¼� �¥ �Ö�Q

�, LcL¤,-8?� L¤!� $}c �! z� !Ë� �!�

 � £¤� ¤¬P� v� �I�! ���. A�z8 9� I»¼

� '»¼� �Âãä� ��� Fig. 48 �Ö×~�. '»¼8?� ù

J A�z� <ÀQR, �� �� 1IÇ� t�8z �$ � 1I�

á� 40 7 �J nJ �á!×8? Â�c®� �7 �¹ nQ

T Á¢PD, 12+� Â�� "� ó�� $}, Â� z, �á!�

$}/b� fg� nQT `o&�. ½[+� �z� �8?� a�+

QT I»¼<� �J �� �Ö×~QR(Table 3), �� 1I�á z

� I»¼8? �¹ nQT <AN�. �c� ��, V�z� A�z

� >�8?� 1I� v� 3 unit/gODPT - � n� ¤[ �, ½

[+ �z� �8?� 3 unit/gODP<� ùJ v� §- A YZ,-

8 +5 � n� ¤[ À�.

3-3. �� � &'�( ��!" %#$ ����� ��

Trichoderma reesei Rut C-308? W:& crude cellulase� �5

� �u67� '»¼ 3WãäQT?, V�z� A�z� p9T ¤7

� 1IÝz� 3 units/gODPT �-XÅ � cH5 YZ1I� Novo-

zym 342 ·� �hI�� `5 � !�� YZ,-� � À�. �

� cH+QT W:P� �� YZ1I�� YZ12 G ½[+ �z

8 @¾� ¿�� '»¼ ,-8? � #$ A 673W,-� 9

»¼* �Sh� ì� ! "� �Ô��. Novozyme 342� �� endo

: exo� �2J 32.2 : 1, ÃÄ8 ��? -& cellulase� 18.7 : 1�R,

¢V{x�1I� papainQT [& 1I� 38.5 : 1T �Ö��.

ÎÎ� YZ��8 ²å V�z� Fig. 68 �Ö×~QR, cH5 1

I� papain [& 1I� �� �J nQT ���. �hI��

`5 � !� YZ ,-� ��, �QT 7+PD � £¤c�

���c�, �J V�z� g$ � �u67� YZX V�z �8?

� ¿�� %� nQT <À�[17]. A�z8?z(Fig. 7), 1I YZ�

�� *�+ YZ��8 �� �J ��� <�R, �� 1I�á8

� A @©£¤� ô� WhP~! �QT Á¢&�. \�� �2�

8?� Table 48 ��� n� �� 1I� `5 � YZ��� =

�+QT �hI�� `5 � YZ��8 ��? �D7� ��� <

�� ��. Cellulase8 �� £¤I ��x�8 ��? @©£¤Ç�

Fig. 3. Freeness with varying enzyme concentrations using either papain- hydrolyzed cellulase(Prep 1) or dialyzed cellulase(Prep 2).

Fig. 4. Brightness of deinking pulp using either papain-hydrolyzed cel-lulase(Prep 1) or dialyzed cellulase(Prep 2) in flotation cells of dif-ferent size.

Fig. 5. Freeness of deinking pulp using either papain-hydrolyzed cellulase(Prep 1) or dialyzed cellulase(Prep 2) in flotation cells of different size.

Table 3. Yield and physical properties of deinked pulp using either pa-pain-hydrolyzed cellulase(Prep 1) or dialyzed cellulase(Prep 2)in flotation cells of different size

Prep 1 Prep 2

Vol. of flotation cells(L) 00.85 8.5 00.85 8.5Yield(%) 89.41 87.32 91.45 87.63

Physicalproperties

Tensile index (Ngm/g)

36.32 41.05 32.43 38.14

Burst index(kPag m2/g)

01.99 02.30 01.89 02.04

Tear index(mNgm2/g)

05.23 05.41 04.13 04.90

HWAHAK KONGHAK Vol. 38, No. 3, June, 2000

Page 5: Mid-Scale Deinking Process for Office Waste Paper ... · Sang-Mok Lee, Keun-Garp Ryu* and Yoon-Mo Koo† Department of Biological Engineering, Inha University, Inchon 402-751, Korea

438 �����������

p

DC,

sey,

,

t� �, Wh& @© £¤� L¤,-X �� ��� �� ÷¥

^P! �8 �2� �I � nQT WÎ&�.

·�, LcL¤X *�+ YZ,-� ��J �hI�� Õ�T ��

Ò�4h�� �áQT �� ,!��� �!� ´Dr! �8 �

2� ��N�� � ��. @©£¤� EF� �z t�8 !A 7

YZ,-� LcL¤X� ©ªX ÷¥ ^P� ¢�� ��. YZ,-

8 ²å EF� ½[+ �z� Table 48 �Ö×~�. î��z� ��

�z�8? Novozym 342� papain [& cellulase� �ø� ���

<ÀQR, crude cellulase� ��� ¼è ½[+ �z� ù¥ �Ö��.

��� ��� =.� !� �� ÎÎ� 1I 5Û×8 �3 � endo

hx� exo hx� }ñ �2� ?T �"! �� nQT WÎ&�.

�c� ��T, 1I8 �� �u67� YZ� �� A�z, V�z�

>�8? �hI�� `5 � YZ8 ��? �� �, ½[+ �z�

��8� �I ùJ ��� <À�. �� 1IYZ��� �� @©£

¤� LcL¤X �ÇQT ú±��! �� nQT <AN�. Papain

¸[& cellulase� ��8� crude cellulase<� �J ½[+ �z�

<�� �Q#T, endoglucanse� �2� �óQTÿ <� �J ½[+

�z� �� � �� n��. ·� cH+QT W:P� �� YZ1

I� Novozym 3428 ��? papain [& 1I� A�z�8? ��

� n� <�� �QR, papain [& cellulase� ��� ½[+ �z

�8? �ø� ��� <�� ��. Trichoderma reesei Rut C-308?

W:& crude cellulase� papainQT ¸[� ��, endo hx� exo hx

� �2�8? cH5 YZ 1I� �ø� ��� <�� �QR, ��

crude cellulase8 �� YZX exo hx� 4h� µX$QTÿ cH

5 YZ1I� �� � �� �J YZ 12� !9� � �� nQ

T o&�.

4. � �

Trichoderma reesei Rut C-308? W:& crude cellulase� papainQ

T ¸[& cellulase� `5 A `s5 �u67 3W� "� YZd

h� #$ À�. Cellulase� endo, exo�28 ²å A�z, V�z,

�2 G ½[+ �z� I»¼ G '»¼8? >- À�, cH+QT

W:P� �� YZ1I Novozym 342� �hI�� `5 � !��

YZ��� '»¼8? � #$ À�. '»¼ YZ8?� 1IÝz

8 ²å A�z� V�z� 1IÝz 3 units/gODP8? p9� <ÀQ

R, I»¼8 � A V�z� ½[+ �z� t� ÀQ� A�z�

�2J �I � ��� <À�. ��� ��� !%QT Trichoderma

reesei Rut C-308? W:& crude cellulase� Ýz� 3 unit/gODPT

�-XÅ �, cH5 YZ1I� Novozym 342 ·� �hI�� `5

� !�� YZ,-� � A ãä� ��, �hI�� �5 �

!�� YZ,-8 ��?� A�z, V�z� �� � ½[+ �z

>�8?� ùJ ��� <À�. �2�8? 1I� `5 � YZ,-

� =�+QT ùJ ��� <À�. Papain [ A EF� ½[+

�z8 ¿�� @¾� cellulase '� endohx� �2� �� ��,

A�z� V�z�8?� cH5 YZ1I(Novozym 342)<� �J 1

2� <�� �QR, ½[+ �z8?z endo� exo� hx�� /b

QT �h�� YZ5 1I� W:� !9� � ��.

º #$� :H� L &-W:!./0`H G 1999'z i( �B

21 H8 � A 7 P~QR, de 7o� ½[+ dh >- _ º

#$� �O8 ��+QT )}� Æ (%)9�EF� h�8 �`*�

+�.

���

1. Kirk, T. K. and Jeffries, T. W.: “Roles for Microbial Enzymes in Pul

and Paper Processing,” ACS Symp. Ser. 655, ACS, Washington

2(1996).

2. Bajpai P. and Bajpai P. K.: Tappi J., 81(12), 111(1998).

3. Jeffries, T. W., Klungness, J. H., Sykes, M. S. and Rutledge-Crop

Fig. 6. Brightness of deinked pulp with different deinking methods(Prep 1: papain-hydrolyzed Rut C-30 cellulase, Prep 2: dialyzedRut C-30 cellulase, Prep 3: Novozym 342, Prep 4: chemicals).

Fig. 7. Brightness of deinked pulp with different deinking methods(Prep 1:papain-hydrolyzed Rut C-30 cellulase, Prep 2: dialyzed Rut C-30 cellulase, Prep 3: Novozym 342, Prep 4: chemicals).

Table 4. Yield and physical properties of deinked pulp with differentdeinking methods(Prep 1: papain hydrolyzed Rut C-30 cellula-se, Prep 2: dialyzed Rut C-30 cellulase, Prep 3: Novozym 342Prep 4: chemicals)

Prep 1 Prep 2 Prep 3 Prep 4

Yield (%) 87.32 87.63 84.99 93.81

Physicalproperties

Tensile index (Ngm/g)

41.05 38.14 38.37 45.58

Burst index (kPagm2/g)

2.30 2.04 2.07 2.47

Tear index (mNgm2/g)

5.41 4.90 6.064.91

���� �38� �3� 2000� 6�

Page 6: Mid-Scale Deinking Process for Office Waste Paper ... · Sang-Mok Lee, Keun-Garp Ryu* and Yoon-Mo Koo† Department of Biological Engineering, Inha University, Inchon 402-751, Korea

�������� � �� ����� ���� 439

d

e

w

K. R.: Tappi J., 77(4), 173(1994).

4. Kim, T. J., Ow, S. S. K. and Eom, T. J.: “Tappi Pulping Conference

Proceedings,” TAPPI PRESS, Atlanta, 1023(1991).

5. Heise, O. U., Uniwin, J. P., Klungness, J. H., Fineran, W. G., Sykes,

M. and Abubakr, S.: Tappi J., 79(3), 207(1996).

6. Tomme, P. H. Van Tilbeurgh, G., Pettersson, Van Damme, J., Vande-

kerckhove, J., Knowles, J., Teeri, T. and Claeyssens, M.: Eur. J. Bio-

chem., 170, 57(1998).

7. Putz, H. J., Renner, K., Göttsching, L. and Jokinen, O.: “Tappi Pulp-

ing Conference Proceedings,” TAPPI PRESS, Atlanta, 877(1994).

8. Heindel, T. J.: Tappi J., 82(31), 115(1998).

9. Fan, L. T., Gharpuray, M. M. and Lee, Y. H.: “Cellulose Hydrolysis,”

Springer-Verlag, Berlin Heidelberg, 21(1987).

10. Klyosov, A. A.: Biochem., 29(47), 10577(1990).

11. Kim, D. W., Chung, Y. K., Jang, Y. H. and Shon, K. H.: Korean J. of

Biotech. Bioeng., 11(6), 718(1996).

12. Kim, B. H. and Jun, Y.: J. of Korea Tappi, 26(2), 23(1994).

13. Sarkar, J. M., Cosper, D. R. and Hartig E. J.: Tappi J., 78(2), 89(1995).

14. Ryu, K. G., Bae, J. S., Lee, S. M. and Koo, Y. M.: Theores and Appli-

cations of Chem. Eng., 5(2), 3165(1999).

15. Stork, G., Pereira, H., Wood, T. M., Düsterhöft, E. M., Toft, A. an

Puls, J.: Tappi J., 78(2), 79(1995).

16. Wood, T. M. and Bhat, K. M.: “Methods for Measuring Cellulas

Activities,” Methods of Enzymology 160, Academic Press Inc., Ne

York, 87(1988).

17. Han, W. S. and Koo, Y. M.: HWAHAK KONGHAK, 36, 759(1998).

HWAHAK KONGHAK Vol. 38, No. 3, June, 2000