Use of Immobilized β-Glucosidase in the Hydrolysis of Cellulose

Woodward, Jonathan; Koran, L.J.; L, Hernàndez; Stephan, Lynette M.; Esen, Asım

doi:10.1021/bk-1993-0533.ch016

Cited by 6 publications

(4 citation statements)

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“…Interestingly, at a w of 0.2 and in an aluminum foil, SA formulation provided a higher retention of β‐glu than that in SAM formulation ( P < 0.05), while there was no difference between SA and SAM formulation when microcapsules were stored at a w of 0.07 and 0.1. The effectiveness of encapsulation technique using alginate‐based formulation on β‐glu stabilization has been reported by Woodward and others (1993).…”

Section: Resultsmentioning

confidence: 99%

Enzyme Stability of Microencapsulated Bifidobacterium animalis ssp. lactis Bb12 after Freeze Drying and during Storage in Low Water Activity at Room Temperature

Dianawati¹,

Shah²

2011

Journal of Food Science

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Stability of enzymes such as β-galactosidase (β-gal), β-glucosidase (β-glu), lactate dehydrogenase (LDH), pyruvate kinase (PK), hexokinase (HK), and ATPase of microencapsulated Bifidobacterium animalis ssp. lactis Bb12 after freeze-drying and after 10 wk of storage at low water activity (a(w)) at room temperature was studied. Bacteria were microencapsulated using alginate formulation with or without mannitol fortification (sodium alginate and mannitol [SAM] and sodium alginate [SA], respectively) by creating gel beads followed by freeze drying. Two types of dried gel beads were then stored at low a(w), such as 0.07, 0.1, and 0.2; storage in an aluminum foil was used as control. All storage was carried out at room temperature of 25 °C for 10 wk. Measurement of β-gal, β-glu, LDH, PK, HK, and ATPase (with or without exposure to pH 2.0 for 2 h) activities was carried out before freeze drying, after freeze drying, and after 10 wk of storage. There was a significant decrease in almost all enzyme activities, except that of PK. SAM and SA showed no different effect on maintaining enzyme activities during freeze drying. Storage for 10 wk at room temperature at various low a(w) using SAM and SA system had a significant effect on retention of most enzymes studied, except that of PK and LDH. Storage at a(w) of 0.07 and 0.1 was more effective in maintaining enzyme activities than storage at a(w) of 0.2 and in an aluminum foil. However, mannitol fortification into alginate system did not significantly improve retention of enzymes during 10 wk of storage.

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Section: Resultsmentioning

confidence: 99%

Enzyme Stability of Microencapsulated Bifidobacterium animalis ssp. lactis Bb12 after Freeze Drying and during Storage in Low Water Activity at Room Temperature

Dianawati¹,

Shah²

2011

Journal of Food Science

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“…The enzyme β-glucosidase is necessary to accomplish further conversion to glucose. β-glucosidase, known also as cellobiose, is a ubiquitous component of cellulases [2]. Given that cellobiose inhibits the reaction, cellulose hydrolysis is greatly impaired.…”

Section: Introductionmentioning

confidence: 99%

“…Published work has showed that supplementation of commercially produced cellulases with β-glucosidase increases the rate and extent of glucose production [3,4]. The native level of β-glucosidase activity in cellulase is, therefore, insufficient for the maximum rate and extent of glucose production to be reached [2]. Since the substrate of β-glucosidase, cellobiose, is water soluble, an immobilized (water-insoluble) enzyme preparation could be used to supplement commercial cellulase/cellulose mixtures, and such immobilized enzyme could be subsequently recovered and reused.…”

Section: Introductionmentioning

confidence: 99%

Stellate MSN-based Dual-enzyme Nano-Biocatalyst for the Cascade Conversion of Non-Food Feedstocks to Food Products

Hsin¹,

Radu²,

Dezayas³

et al. 2017

J Thermodyn Catal

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The successful demonstration of a tandem enzymatic catalyst which utilizes stellate macroporous silica nanospheres (Stellate MSN) platform as dual-enzyme host is reported herein. Upon simultaneous loading of beta-glucosidase and glucose isomerase inside their porous structure, Stellate MSNs-featuring a hierarchical pore arrangement and large surface area, show capability to perform a cascade reaction that converts cellobiose, a cellulosic hydrolysis product, into glucose and further to fructose. The silica platform provides a modality for substrate channelling which involves the transfer of the cascade intermediate, glucose, to the next enzyme without first diffusing to the bulk. A key aspect to this proof-of-concept is the two-enzyme system working in an optimized pH domain to fit the modus operandi for both enzymes. The concept could be extrapolated to other enzyme tandems, with potential to impact dramatically enzymatic processes which require multi-catalyst, one-pot transformations.

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“…Microencapsulated b-gal was preserved well after three weeks of storage in aqueous solution at 4 C and pH 7.0; decrease in activity was below 5%. Woodward et al (1993) found that microencapsulated ß-glu using propylene glycol alginate/bone gelatin was stable during exposure to 40 C for couple months without losing its effectiveness. Li et al (2011a) demonstrated that ATPase of L. reuteri protected by trehalose or RSM decreased significantly during freeze drying compared to pyruvate kinase and hexokinase.…”

Section: Enzyme Activities Of Microencapsulated Bacteriamentioning

confidence: 99%

Survival of Microencapsulated Probiotic Bacteria after Processing and during Storage: A Review

Dianawati

Mishra

Shah

2015

Critical Reviews in Food Science and Nutrition

118

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The use of live probiotic bacteria as food supplement has become popular. Capability of probiotic bacteria to be kept at room temperature becomes necessary for customer's convenience and manufacturer's cost reduction. Hence, production of dried form of probiotic bacteria is important. Two common drying methods commonly used for microencapsulation are freeze drying and spray drying. In spite of their benefits, both methods have adverse effects on cell membrane integrity and protein structures resulting in decrease in bacterial viability. Microencapsulation of probiotic bacteria has been a promising technology to ensure bacterial stability during the drying process and to preserve their viability during storage without significantly losing their functional properties such acid tolerance, bile tolerance, surface hydrophobicity, and enzyme activities. Storage at room temperatures instead of freezing or low temperature storage is preferable for minimizing costs of handling, transportation, and storage. Concepts of water activity and glass transition become important in terms of determination of bacterial survival during the storage. The effectiveness of microencapsulation is also affected by microcapsule materials. Carbohydrate- and protein-based microencapsulants and their combination are discussed in terms of their protecting effect on probiotic bacteria during dehydration, during exposure to harsh gastrointestinal transit and small intestine transit and during storage.

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Use of Immobilized β-Glucosidase in the Hydrolysis of Cellulose

Cited by 6 publications

References 0 publications

Enzyme Stability of Microencapsulated Bifidobacterium animalis ssp. lactis Bb12 after Freeze Drying and during Storage in Low Water Activity at Room Temperature

Enzyme Stability of Microencapsulated Bifidobacterium animalis ssp. lactis Bb12 after Freeze Drying and during Storage in Low Water Activity at Room Temperature

Stellate MSN-based Dual-enzyme Nano-Biocatalyst for the Cascade Conversion of Non-Food Feedstocks to Food Products

Survival of Microencapsulated Probiotic Bacteria after Processing and during Storage: A Review

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