Pullulanase type II from a local Bacillus isolate H1.5 : isolation, production and characterization of the enzyme

Enzymes that specifically break down the branch points – debranching enzymes – have been known for more than a decade. Pullulanase (EC 3.2.1.41, pullulan 6- glucanohydrolase), which was first reported in Aerobacter aerogenes splits the α-1,6- glucosidic linkages in pullulan and give rise finally to...

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Main Authors: Hii, Siew Ling, Ling, Tau Chuan, Mohammad, Rosfarizan, Ariff, Arbakariya
Other Authors: Ahmad, Abdul Latif
Format: Book Section
Language:English
Published: Penerbit Universiti Sains Malaysia 2004
Subjects:
Online Access:http://eprints.usm.my/42186/
http://eprints.usm.my/42186/1/pBIO09.pdf
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author Hii, Siew Ling
Ling, Tau Chuan
Mohammad, Rosfarizan
Ariff, Arbakariya
author2 Ahmad, Abdul Latif
author_facet Ahmad, Abdul Latif
Hii, Siew Ling
Ling, Tau Chuan
Mohammad, Rosfarizan
Ariff, Arbakariya
author_sort Hii, Siew Ling
building USM Institutional Repository
collection Online Access
description Enzymes that specifically break down the branch points – debranching enzymes – have been known for more than a decade. Pullulanase (EC 3.2.1.41, pullulan 6- glucanohydrolase), which was first reported in Aerobacter aerogenes splits the α-1,6- glucosidic linkages in pullulan and give rise finally to maltotriose (Yuzuru and Masaharu, 1983). In most cases, pullulanase can also cleave the α-1,6 link of other branched polysaccharides, such as starch, glycogen and maltodextrin
first_indexed 2025-11-15T17:48:05Z
format Book Section
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institution Universiti Sains Malaysia
institution_category Local University
language English
last_indexed 2025-11-15T17:48:05Z
publishDate 2004
publisher Penerbit Universiti Sains Malaysia
recordtype eprints
repository_type Digital Repository
spelling usm-421862018-10-31T03:55:42Z http://eprints.usm.my/42186/ Pullulanase type II from a local Bacillus isolate H1.5 : isolation, production and characterization of the enzyme Hii, Siew Ling Ling, Tau Chuan Mohammad, Rosfarizan Ariff, Arbakariya Q179.9-180 Research Enzymes that specifically break down the branch points – debranching enzymes – have been known for more than a decade. Pullulanase (EC 3.2.1.41, pullulan 6- glucanohydrolase), which was first reported in Aerobacter aerogenes splits the α-1,6- glucosidic linkages in pullulan and give rise finally to maltotriose (Yuzuru and Masaharu, 1983). In most cases, pullulanase can also cleave the α-1,6 link of other branched polysaccharides, such as starch, glycogen and maltodextrin Penerbit Universiti Sains Malaysia Ahmad, Abdul Latif Yahya, Ahmad Rahim Mohd Abdullah, Amirul AI-Ashraf Muhammad, Tengku Sifzizul Tengku 2004 Book Section PeerReviewed application/pdf en http://eprints.usm.my/42186/1/pBIO09.pdf Hii, Siew Ling and Ling, Tau Chuan and Mohammad, Rosfarizan and Ariff, Arbakariya (2004) Pullulanase type II from a local Bacillus isolate H1.5 : isolation, production and characterization of the enzyme. In: The 4th Annual Seminar of National Science Fellowship NSF 2004 Proceedings. Penerbit Universiti Sains Malaysia, Pulau Pinang, Malaysia, pp. 49-53.
spellingShingle Q179.9-180 Research
Hii, Siew Ling
Ling, Tau Chuan
Mohammad, Rosfarizan
Ariff, Arbakariya
Pullulanase type II from a local Bacillus isolate H1.5 : isolation, production and characterization of the enzyme
title Pullulanase type II from a local Bacillus isolate H1.5 : isolation, production and characterization of the enzyme
title_full Pullulanase type II from a local Bacillus isolate H1.5 : isolation, production and characterization of the enzyme
title_fullStr Pullulanase type II from a local Bacillus isolate H1.5 : isolation, production and characterization of the enzyme
title_full_unstemmed Pullulanase type II from a local Bacillus isolate H1.5 : isolation, production and characterization of the enzyme
title_short Pullulanase type II from a local Bacillus isolate H1.5 : isolation, production and characterization of the enzyme
title_sort pullulanase type ii from a local bacillus isolate h1.5 : isolation, production and characterization of the enzyme
topic Q179.9-180 Research
url http://eprints.usm.my/42186/
http://eprints.usm.my/42186/1/pBIO09.pdf