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Microbial Pullulan: Properties, Bioprocess Engineering, and Applications
Published in Shakeel Ahmed, Aisverya Soundararajan, Pullulan, 2020
Sugumaran Karuppiah, Sameeha Syed Abdul Rahman, V. Ponnusami
Pullulanase (EC.3.2.1.41, pullulan 6-glucanohydrolase) is a hydrolytic, debranching, and thermostable enzyme, which belongs to the family of glycosyl hydrolases thirteen (GH13). It is widely present in various plants, animals, and microorganisms such as bacteria and fungi. Pullulan and other amylaceous polysaccharides containing α-(1→6) glycosidic linkages were hydrolyzed by this enzyme to yield maltotriose, a major product and maltotetraose, a by-product under suitable conditions [70, 71]. The mechanism of the enzymatic reaction for amylaceous type of polysaccharides or pullulan degradation and their end products are different in each case [72].
Produced by Recombinant Bacteria
Published in Yoshikatsu Murooka, Tadayuki Imanaka, Recombinant Microbes for Industrial and Agricultural Applications, 2020
Debranching enzymes hydrolyze the α-l,6-glucosidic linkages of starch and are present in higher plants and microorganisms. Isoamylase (EC 3.2.1.68; glycogen 6-glucanohydrolase), pullulanase (EC 3.2.1.41; pullulan 6-glucanohydrolase), and amylo-1,6-glucosidase (EC 3.2.1.33) belong to this group of enzymes. They are useful for structural analysis of starch, glycogen, pullulan, and other saccharides. Isoamylase and pullulanase are used industrially to produce glucose or maltose from starch in combination with glucoamylase or β-amylase, respectively.
Purification and biochemical characterization of pullulanase produced from Bacillus sp. modified by ethyl-methyl sulfonate for improved applications
Published in Preparative Biochemistry & Biotechnology, 2023
Oladipo O. Olaniyi, Blessing Oriade, Olusola T. Lawal, Adeyemi O. Ayodeji, Yetunde O. Olorunfemi, Festus O. Igbe
An extracellular carbohydrase called pullulanase debranches the extracellular yeast polysaccharide known as pullulan to produce maltotriose (EC 3.2.1.41)[1]. Pullulanase was first isolated from the mesophilic bacteria Klebsiella pneumonia by Bender and Wallenfels in 1961[2,3]. Curiosity has been sparked by the peculiar activity of microbial pullulanase on α-1, 6 linkages in pullulan, a linear α-glucan predominantly consisting of maltotriosyl units connected by α-1, 6 -bonds. Pullulanase has numerous uses, making it very significant. It is an enzyme that breaks down starch into glucose and maltose. Pullulanase has been reported to be employed on a wide scale in the conversion of starch to glucose and maltose, which are used more efficiently in the manufacturing of glucose sirup[4]. It is commonly utilized in the industry for starch saccharification. Pullulanase is also utilized in the detergent business[5], baking, and the manufacturing of cyclodextrins, which are used in biotechnological products and low-calorie beer[6].
Characterization of a novel detergent-resistant type I pullulanase from Bacillus megaterium Y103 and its application in laundry detergent
Published in Preparative Biochemistry & Biotechnology, 2023
Yongmin Wu, Shuai Huang, Xiaobo Liang, Peng Han, Yuchun Liu
Pullulanase (EC 3.2.1.41) is one of debranching enzymes which could cleave α-1,6-glycosidic linkages in pullulan and starch-type polysaccharides. According to substrate specificity and hydrolytic property, pullulanases are classified as five types viz, type I, type II, and pullulan hydrolases (types I, II, and III).[1] According to amino sequence, the type I and II pullulanases are categorized into GH13 and GH57, respectively, pullulan hydrolases of types I and III are grouped in GH13, and the type II pullulan hydrolases belong to GH49; pullulanases in GH13 usually contain four conserved regions (I–IV).[2] Type I pullulanases contain the consensus sequence YNWGYDP.[3] In general, pullulanases are used to catalyze hydrolysis reaction. However, several pullulanases have transglycosylation activity[1,4–6] and few of them can form α-1,4-glucosidic linkage.[1,4]
Optimization and characterization of pullulan production by a newly isolated high-yielding strain Aureobasidium melanogenum
Published in Preparative Biochemistry and Biotechnology, 2019
Guoqiang Chen, Youshuang Zhu, Ge Zhang, Haobao Liu, Yuxi Wei, Pinggui Wang, Fan Wang, Mo Xian, Haiying Xiang, Haibo Zhang
Pullulan is connected by α-1,6-D-glucosidic and α-1,4-D-glucosidic linkages,[18] and pullulanase could selectively hydrolyze α-1,6-D-glucosidic linkages of pullulan and EPS to form maltotriose.[20] In the present study, the purified EPS and pullulan (sigma) with or without the hydrolysis of pullulanase and maltotriose were migrated with a suitable developing agent onto the TLC plate (Fig. 2). After migration of the samples in above developing agent. Pullulan (lane 1) and purified EPS (lane 5) with high MW, which could not be expanded with the developing agent. Contrarily, with pullulanase hydrolysis of pullulan (lane 2) and purified EPS (lane 4) to maltotriose appeared the same spot onto the TLC plate as well as the control of maltotriose (lane 3 of 10 mg/mL). The results showed that the major component of purified EPS was pullulan.