Protein-peptide nutritional material prepared from surimi wash-water using immobilized chymotrypsin-trypsin

Ding, Haiyan; Li, Dongfang; Wei, Xiaoyi; Huang, Yao-Wen; Cui, Shuai; Zhou, Tao

doi:10.1002/jsfa.7969

Cited by 9 publications

(8 citation statements)

References 16 publications

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“…Mammalian trypsin is generally utilized for the preparation of insulin from its precursor because of the canonical tryptic cleavage of lysine to remove the C-chain [4,41]. Most commercial trypsin is extracted from the mammalian pancreas, which carries the risks of bioactive compound contaminants, infectious viruses, and health-harming proteases [42].…”

Section: Application Of High Yield Trypsin To Processing Of the Insulmentioning

confidence: 99%

Improving production of Streptomyces griseus trypsin for enzymatic processing of insulin precursor

Zhang

Liang

Zhang³

et al. 2020

Microb Cell Fact

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Background: Trypsin has many applications in food and pharmaceutical manufacturing. Although commercial trypsin is usually extracted from porcine pancreas, this source carries the risks of infectivity and immunogenicity. Microbial Streptomyces griseus trypsin (SGT) is a prime alternative because it possesses efficient hydrolysis activity without such risks. However, the remarkable hydrolysis efficiency of SGT causes autolysis, and five autolysis sites, R21, R32, K122, R153, and R201, were identified from its autolysate. Results: The tbcf (K101A, R201V) mutant was screened by a directed selection approach for improved activity in flask culture (60.85 ± 3.42 U mL −1 , increased 1.5-fold). From the molecular dynamics simulation, in the K101A/R201V mutant the distance between the catalytical residues D102 and H57 was shortened to 6.5 Å vs 7.0 Å in the wild type, which afforded the improved specific activity of 1527.96 ± 62.81 U mg −1. Furthermore, the production of trypsin was increased by 302.8% (689.47 ± 6.78 U mL −1) in a 3-L bioreactor, with co-overexpression of chaperones SSO2 and UBC1 in Pichia pastoris. Conclusions: SGT protein could be a good source of trypsin for insulin production. As a result of the hydrolysates analysis and direct selection, the activity of the tbcf (K101A, R201V) mutant increased 1.5-fold. Furthermore, the production of trypsin was improved threefold by overexpressing chaperone protein in Pichia pastoris. Future studies should investigate the application of SGT to insulin and pharmaceutical manufacturing.

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Section: Application Of High Yield Trypsin To Processing Of the Insulmentioning

confidence: 99%

Improving production of Streptomyces griseus trypsin for enzymatic processing of insulin precursor

Zhang

Liang

Zhang³

et al. 2020

Microb Cell Fact

View full text Add to dashboard Cite

show abstract

“…The mammalian trypsin was generally applied for the preparing insulin from its precursor, because of the canonically tryptic cleavage of lysine for removal of C-chain [4,40]. While, the traditional method for preparing trypsin is extraction from the mammalian pancreas, which has the risk of the bioactive compound, infectious virus, and heath-harmful proteases [41].…”

Section: Application Of High-yield Trypsin To Processing Insulin Precmentioning

confidence: 99%

Improving production of Streptomyces griseus trypsin for its application in processing insulin precursor

Zhang

Liang

Zhang³

et al. 2019

Preprint

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Background: Trypsin has a plenty application in food and pharmaceutical manufacture. While, the commercial trypsin is usually extracted from pork pancreas, which has the risk of infectious and immunogenicity. Therefore, the microbial Streptomyces griseus trypsin (SGT) is a prior alternation because it processes efficient hydrolysis activity without the aforementioned risk. The remarkable hydrolysis efficiency of SGT caused its autolysis, and five autolysis sites R21, R32, K122, R153, and R201 were identified from its' autolysate. Results: The tbcf (K101A, R201V) mutant was screened by directed selection approach for improved activity in flask culture (60.85 ± 3.42 U·mL -1 , increased 1.5-fold). From the molecular dynamics simulation, the K101A/R201V mutation shortened the distant between catalytical residues D102 and H57 from 6.5 Å vs 7.0 Å, which afforded the improved specific activity 1527.96 ± 62.81 U·mg -1 . Further, the production of trypsin was increased 302.8% (689.47 ± 6.78 U·mL −1 ) in 3-L bio-reactor, with co-overexpression of chaperones SSO2 and UBC1 in Pichia pastoris. Conclusions: The SGT protein could be an adequate trypsin for insulin production. When working with hydrolysates analysis and direction selection, the tbcf (K101A, R201V) mutant increased 1.5-fold activity. Further, the production of trypsin was improved 3-fold by overexpressing chaperone protein in Pichia pastoris . The future study should be emphasized on the application of SGT in insulin manufacture and pharmaceutical.

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“…The washing operations carried out in the manufacture of surimi eliminate large amounts of proteins. Ot is estimated that, in an annual production of 200.00 tonnes of surimi, more than 6.000 tonnes of protein residues are eliminated, which means loss of nutrients and increase in treatment steps and costs for effluent disposal (Ding et al, 2017;Lin et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

Enrichment of fishburgers with proteins from surimi washing water

et al. 2020

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The proteins recovered by ultrafiltration (UF) represent a co-product of fish industrialization and can be used as a protein ingredient in the fortification of food formulations. The objective of this study was to evaluate the quality of surimi fishburger elaborated with the proteins recovered by UF from the wastewater generated in the production of surimi. The water generated in the washing operations of trims of farmed tilapia (Oreochromis niloticus) were filtered in a 30 kDa polyethersulfone membrane. The recovered proteins were dehydrated in spray dryer and added at 5 and 10% into fishburgers made with tilapia surimi. The fishburgers were evaluated for proximal composition, cooking yield, sensory parameters and acceptability. The incorporation of proteins into the fishburgers improved the sensory aspects of the final product and provided greater acceptability while maintaining the same manufacturing yield. The addition of 10% of the recovered proteins increased the nutritional value of surimi fishburgers. Practical Application:The recovery of proteins from surimi wastewaters reduces organic matter, makes the production process more profitable and less aggressive to environment and, in addition, provides a protein-rich ingredient that may find use in food industry. The use of this protein concentrate in food products like surimi increases nutritional quality and productivity and so may reach consumers and producers demands.

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Protein-peptide nutritional material prepared from surimi wash-water using immobilized chymotrypsin-trypsin

Abstract: An efficient and practical protocol for the recovery of protein from hairtail surimi wash-water has been developed. The PPNM prepared in this work could be used as a nutraceutical and as an ingredient of functional foods. © 2016 Society of Chemical Industry.

Cited by 9 publications

References 16 publications

Improving production of Streptomyces griseus trypsin for enzymatic processing of insulin precursor

Improving production of Streptomyces griseus trypsin for enzymatic processing of insulin precursor

Improving production of Streptomyces griseus trypsin for its application in processing insulin precursor

Enrichment of fishburgers with proteins from surimi washing water

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