Cellulases: Characteristics, Sources, Production, and Applications

Zhang, Xiaozhou; Zhang, Y.‐H. Percival

doi:10.1002/9781118642047.ch8

Cited by 108 publications

(74 citation statements)

References 118 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The first discovered and best characterized GH7 CBH was from the industrial workhorse Trichoderma reesei [1, 3]; since then, GH7 CBH from T. reesei has been one of the major components of commercial cellulase cocktails [4, 11, 12]. Albeit, reports of alternatives with higher potentials—higher specific activity, less inhibition to cellobiose and lignin-derived compounds—from genus Penicillium , Humicola , Acremonium among others abound [4].…”

Section: Introductionmentioning

confidence: 99%

Comparative insights into the saccharification potentials of a relatively unexplored but robust Penicillium funiculosum glycoside hydrolase 7 cellobiohydrolase

Ogunmolu

Jagadeesha

Kumar

et al. 2017

Biotechnol Biofuels

View full text Add to dashboard Cite

BackgroundGH7 cellobiohydrolases (CBH1) are vital for the breakdown of cellulose. We had previously observed the enzyme as the most dominant protein in the active cellulose-hydrolyzing secretome of the hypercellulolytic ascomycete—Penicillium funiculosum (NCIM1228). To understand its contributions to cellulosic biomass saccharification in comparison with GH7 cellobiohydrolase from the industrial workhorse—Trichoderma reesei, we natively purified and functionally characterized the only GH7 cellobiohydrolase identified and present in the genome of the fungus.ResultsThere were marginal differences observed in the stability of both enzymes, with P. funiculosum (PfCBH1) showing an optimal thermal midpoint (T m) of 68 °C at pH 4.4 as against an optimal T m of 65 °C at pH 4.7 for T. reesei (TrCBH1). Nevertheless, PfCBH1 had an approximate threefold lower binding affinity (K m), an 18-fold higher turnover rate (k cat), a sixfold higher catalytic efficiency as well as a 26-fold higher enzyme-inhibitor complex equilibrium dissociation constant (K i) than TrCBH1 on p-nitrophenyl-β-d-lactopyranoside (pNPL). Although both enzymes hydrolyzed cellooligomers (G2–G6) and microcrystalline cellulose, releasing cellobiose and glucose as the major products, the propensity was more with PfCBH1. We equally observed this trend during the hydrolysis of pretreated wheat straws in tandem with other core cellulases under the same conditions. Molecular dynamic simulations conducted on a homology model built using the TrCBH1 structure (PDB ID: 8CEL) as a template enabled us to directly examine the effects of substrate and products on the protein dynamics. While the catalytic triads—EXDXXE motifs—were conserved between the two enzymes, subtle variations in regions enclosing the catalytic path were observed, and relations to functionality highlighted.ConclusionTo the best of our knowledge, this is the first report about a comprehensive and comparative description of CBH1 from hypercellulolytic ascomycete—P. funiculosum NCIM1228, against the backdrop of the same enzyme from the industrial workhorse—T. reesei. Our study reveals PfCBH1 as a viable alternative for CBH1 from T. reesei in industrial cellulase cocktails.Electronic supplementary materialThe online version of this article (doi:10.1186/s13068-017-0752-x) contains supplementary material, which is available to authorized users.

show abstract

Section: Introductionmentioning

confidence: 99%

Comparative insights into the saccharification potentials of a relatively unexplored but robust Penicillium funiculosum glycoside hydrolase 7 cellobiohydrolase

Ogunmolu

Jagadeesha

Kumar

et al. 2017

Biotechnol Biofuels

View full text Add to dashboard Cite

show abstract

“…Because the cellulase complex has a broad spectrum of catalytic mechanisms, it was classified as glycoside hydrolases (EC 3.2.1.‐) with family numbers 1, 3, 5, 6, 7, 8, 9, 12, 26, 44, 45, 48, and 51. Family numbers 61 and 74 were also proposed owing to a cellulase like activity (Zhang and Zhang ). In cellulose hydrolysis, endoglucanase (EG) and exoglucanase (CBG) enzymes 1st work synergistically to transform cellulose into small cellooligosaccharides, and then β‐glucosidase (BG) hydrolyzes the cello‐oligosaccharides into simple sugars or glucoses (Sathya and Khan ; Sindhu and others ).…”

Section: Lignocellulosic Substrates and Degrading Enzymesmentioning

confidence: 99%

Functional Applications of Lignocellulolytic Enzymes in the Fruit and Vegetable Processing Industries

Toushik

Lee

et al. 2017

Journal of Food Science

View full text Add to dashboard Cite

Cellulose, hemicellulose, pectin (carbohydrate), and lignin (noncarbohydrate) polymers are the main substrates of lignocellulose-degrading enzymes. They are present in large amounts in the primary cell wall and dietary fibers of major fruits and vegetables. During processing of fruits and vegetables to the corresponding final food products, lignocellulosic substrates are hydrolyzed by different lignocellulolytic enzymes. Currently, lignocellulolytic enzymes such as cellulases, xylanases, pectinases, and laccases are extensively used during the processing of fruits and vegetables, in applications like texturizing and flavoring of products in the food industries. The present article provides an updated overview of functional applications of lignocellulolytic enzymes in the juice processing, oil extraction, and alcoholic beverage processing industries. Extensive use of lignocellulolytic enzymes in different food processing industries not only accelerates the production rates but also improves product quality. It is also possible to ensure the efficient use of fruits and vegetables globally by employing lignocellulolytic enzymes in the corresponding processing industries to convert them into food commodities, which will not only raise their economic value in the global market but also increase food availability, which will help mitigate nutritional problems worldwide.

show abstract

“…Selulase merupakan nama kelompok enzim yang memutuskan ikatan glikosidik beta-1,4 di dalam selulosa, selodekstrin, selobiosa, dan turunan selulosa lainnya. Selulase terdiri dari enzim -enzim yang bekerja bersama-sama secara sinergis untuk menghidrolisis selulosa (Zhang & Zhang, 2013).…”

Section: Seleksi Dan Identifikasi Bakteri Selulolitik Pendegradasi Daunclassified

Seleksi dan Identifikasi Bakteri Selulolitik yang Dapat Mendegradasi Serat Kasar Daun Singkong

Mulyasari

Widanarni

Suprayudi

et al. 2015

JPBKP

View full text Add to dashboard Cite

ABSTRAKPemanfaatan daun singkong sebagai bahan baku pakan ikan belum dilaksanakan secara optimal karena mengandung selulosa yang cukup tinggi. Tuj uan penelitian ini adalah mendapatkan bakteri yang dapat mendegradasi serat daun singkong dan melakukan identifikasi jenis bakteri selulolitik tersebut. Seleksi bakteri selulolitik dilakukan pada 4 jenis isolat bakteri asal saluran pencernaan ikan gurame yaitu UG3, UG6, UG7, dan UG8 dengan mengukur aktivitas enzim selulase secara kuantitatif pada substrat Carboxy Methyl Cellulose (CMC) dan daun singkong menggunakan metode 3,5-dinitrosalicylic acid (DNS). Identifikasi bakteri dilakukan pada 3 isolat yang memiliki aktivitas enzim selulase tertinggi pada substrat daun singkong berdasarkan morfologi (perwarnaan Gram, motilitas dan bentuk bakteri), uji biokimia (oksidase dan katalase) dan analisis gen (16S-rRNA). Hasil penelitian menunjukkan bahwa dari 4 isolat yang diuji cobakan, isolat UG7 memiliki aktivitas enzim selulase (CMCase) tertinggi (0,0043 U/ ml) sedangkan yang terendah adalah UG3 (0,0018 U/ml). Pada uji coba di substrat daun singkong, aktivitas enzim tertinggi terlihat pada isolat UG3 (0,107 U/ml) dan terendah adalah UG6 (0,077 U/ ml). Hasil identifikasi dari 3 jenis isolat bakteri uji yang memiliki kemampuan mendegradasi daun singkong tertinggi (UG3, UG7, dan UG8) menunjukkan bahwa ketiga jenis isolat tersebut merupakan bakteri jenis Gram positif berbentuk batang (basil). Berdasarkan data base dari GenBank, isolat UG3 memiliki kemiripan sebesar 93% dengan Bacillus clausii, UG7 memiliki kemiripan sebesar 96% dengan Bacillus amyloliquefaciens dan UG8 memiliki kemiripan sebesar 88% dengan Bacillus subtilis.

show abstract

Cellulases: Characteristics, Sources, Production, and Applications

Cited by 108 publications

References 118 publications

Comparative insights into the saccharification potentials of a relatively unexplored but robust Penicillium funiculosum glycoside hydrolase 7 cellobiohydrolase

Comparative insights into the saccharification potentials of a relatively unexplored but robust Penicillium funiculosum glycoside hydrolase 7 cellobiohydrolase

Functional Applications of Lignocellulolytic Enzymes in the Fruit and Vegetable Processing Industries

Seleksi dan Identifikasi Bakteri Selulolitik yang Dapat Mendegradasi Serat Kasar Daun Singkong

Contact Info

Product

Resources

About